Randal J. Kaufman

From endoplasmic-reticulum stress to the inflammatory response (2008)

Zhang, Kezhong, Kaufman, Randal J.

The endoplasmic reticulum is responsible for much of a cell's protein synthesis and folding, but it also has an important role in sensing cellular stress. Recently, it has been shown that the...

An efficient in vitro translation system from mammalian cells lacking the translational inhibition caused by eIF2 phosphorylation. (2008)

Zeenko, Vladimir V., Wang, Chuanping, Majumder, Mithu, Komar, Anton A., Snider, Martin D., Merrick, William C., ...

In vitro translation systems are used to investigate translational mechanisms and to synthesize proteins for characterization. Most available mammalian cell-free systems have reduced efficiency due...

Human HRD1 Promoter Carries a Functional Unfolded Protein Response Element to Which XBP1 but not ATF6 Directly Binds (2008)

Yamamoto, Keisuke, Suzuki, Natsumi, Wada, Tadashi, Okada, Tetsuya, Yoshida, Hiderou, Kaufman, Randal J., ...

Quality control of proteins in the endoplasmic reticulum (ER) is achieved by two mechanisms, the productive folding mechanism, which is assisted by a number of ER-localized molecular chaperones and...

An efficient in vitro translation system from mammalian cells lacking the translational inhibition caused by eIF2 phosphorylation (2008)

Zeenko, Vladimir V., Wang, Chuanping, Majumder, Mithu, Komar, Anton A., Snider, Martin D., Merrick, William C., ...

In vitro translation systems are used to investigate translational mechanisms and to synthesize proteins for characterization. Most available mammalian cell-free systems have reduced efficiency due...

Glucose activates a protein phosphatase-1-mediated signaling pathway to enhance overall translation in pancreatic beta-cells (2006)

Scheuner, Donalyn, Patel, Rupali, Song, Benbo, ...

Both the rate of overall translation and the specific acceleration of proinsulin synthesis are known to be glucose regulated processes in the beta cell. In this study we propose that glucose-induced...

Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins (2006)

D. Thomas Rutkowski, Stacey M. Arnold, Corey N. Miller, Jun Wu, Jack Li, Kathryn M. Gunnison, ...

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) activates a signaling cascade known as the unfolded protein response (UPR). Although activation of the UPR is well described,...

Initiation of protein synthesis by hepatitis C virus is refractory to reduced eIF2.GTP.Met-tRNA(i)(Met) ternary complex availability. (2006)

Robert, Francis, Kapp, Lee D., Khan, Shakila N., Acker, Michael G., Kolitz, Sarah, Kazemi, Shirin, ...

A cornerstone of the antiviral interferon response is phosphorylation of eukaryotic initiation factor (eIF)2alpha. This limits the availability of eIF2.GTP.Met-tRNA(i)(Met) ternary complexes, reduces...

Combined deficiency of factor V and factor VIII is due to mutations in either LMAN1 or MCFD2. (2006)

Zhang, Bin, McGee, Beth, Yamaoka, Jennifer S., Guglielmone, Hugo, Downes, Katharine A., Minoldo, Salvador, ...

Mutations in LMAN1 (ERGIC-53) or MCFD2 cause combined deficiency of factor V and factor VIII (F5F8D). LMAN1 and MCFD2 form a protein complex that functions as a cargo receptor ferrying FV and FVIII...

Genetic Interactions Due to Constitutive and Inducible Gene Regulation Mediated by the Unfolded Protein Response in C. elegans (2005)

Xiaohua Shen, Ronald E. Ellis, Kenjiro Sakaki, Randal J. Kaufman

The unfolded protein response (UPR) is an adaptive signaling pathway utilized to sense and alleviate the stress of protein folding in the endoplasmic reticulum (ER). In mammals, the UPR is mediated...

Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis (2005)

Mierde, Dirk Vander, Song, Benbo, Flamez, Daisy, ...

Type 2 diabetes is a disorder of hyperglycemia resulting from failure of beta cells to produce adequate insulin to accommodate an increased metabolic demand. Here we show that regulation of mRNA...

Differential Contributions of ATF6 and XBP1 to the Activation of Endoplasmic Reticulum Stress-Responsive cis-Acting Elements ERSE, UPRE and ERSE-II (2004)

Yamamoto, Keisuke, Yoshida, Hiderou, Kokame, Koichi, Kaufman, Randal J., Mori, Kazutoshi

ATF6 and XBP1 are transcription factors activated specifically in response to endoplasmic reticulum (ER) stress. Three cis-acting elements capable of binding to ATF6, XBP1 or both have been...

Control of gene expression at the level of translation initiation (1994)

Kaufman, Randal J

Protein synthesis is controlled at the level of translation initiation. Cells rapidly respond to environmental changes by disassembly of polysomes and recruitment of specific mRNAs from inactive...

The Levels of Endoplasmic Reticulum Proteins and ATP Affect Folding and Secretion of Selective Proteins (1994)

Dorner, Andrew J., Kaufman, Randal J.

Abstract. Proteins transiting the endoplasmic reticulum (ER) interact with a number of lumenal proteins, such as the glucose regulated proteins (GRPs), that either facilitate or prohibit protein...

Improved vectors for stable expression of foreign genes in mammalian cells by use of the untranslated leader sequence from EMC virus (1991)

Kaufman, Randal J., Davies, Monique V., Wasley, Louise C., Michnick, Donna

Dicistronic mRNA expression vectors efficiently translate a 5′ open reading frame (ORF) and contain a selectable marker within the 3′ end which is inefficiently translated. In these vectors, the...

Highly inducible expression from vectors containing multiple GRE's in CHO cells overexpressing the glucocorticoid receptor (1989)

Israel, David I., Kaufman, Randal J.

A conditional glucocorticoid-responsive expression vector system is described for highly inducible expression of heterologous genes in mammalian cells. This host-vector system requires high level...

Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p

Welihinda, Ajith A., Tirasophon, Witoon, Green, Sarah R., Kaufman, Randal J.

In eukaryotic cells, accumulation of unfolded protein in the endoplasmic reticulum induces transcription of a family of genes encoding endoplasmic reticulum protein chaperones through a conserved...

Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa

Pipe, Steven W., Kaufman, Randal J.

Individuals with hemophilia A require frequent infusion of preparations of coagulation factor VIII. The activity of factor VIII (FVIII) as a cofactor for factor IXa in the coagulation cascade is...

Double-Stranded RNA-Activated Protein Kinase (PKR) Is Negatively Regulated by 60S Ribosomal Subunit Protein L18

Kumar, Kotlo U., Srivastava, Sri P., Kaufman, Randal J.

The double-stranded RNA (dsRNA)-activated protein kinase (PKR) provides a fundamental control step in the regulation of protein synthesis initiation through phosphorylation of the alpha subunit of...

Regulation of starvation- and virus-induced autophagy by the eIF2α kinase signaling pathway

Tallóczy, Zsolt, Jiang, Wenxia, Virgin, Herbert W., Leib, David A., Scheuner, Donalyn, Kaufman, Randal J., ...

The eIF2α kinases are a family of evolutionarily conserved serine/threonine kinases that regulate stress-induced translational arrest. Here, we demonstrate that the yeast eIF2α kinase, GCN2, the...

Protein Serine/Threonine Phosphatase Ptc2p Negatively Regulates the Unfolded-Protein Response by Dephosphorylating Ire1p Kinase

Welihinda, Ajith A., Tirasophon, Witoon, Green, Sarah R., Kaufman, Randal J.

Cells respond to the accumulation of unfolded proteins in the endoplasmic reticulum (ER) by increasing the transcription of the genes encoding ER-resident chaperone proteins. Ire1p is a transmembrane...

In Vivo Replication of an ICP34.5 Second-Site Suppressor Mutant following Corneal Infection Correlates with In Vitro Regulation of eIF2α Phosphorylation

Ward, Stephen L., Scheuner, Donalyn, Poppers, Jeremy, Kaufman, Randal J., Mohr, Ian, Leib, David A.

In animal models of herpes simplex virus type 1 (HSV-1) infection, ICP34.5-null viruses are avirulent and also fail to grow in a variety of cultured cells due to their inability to prevent...

Optimization of protease-inhibitor interactions by randomizing adventitious contacts

Komiyama, Tomoko, VanderLugt, Bryan, Fugère, Martin, Day, Robert, Kaufman, Randal J., Fuller, Robert S.

Polypeptide protease inhibitors are often found to inhibit targets with which they did not coevolve, as in the case of high-affinity inhibition of bacterial subtilisin by the leech inhibitor eglin c....

Phosphorylation of the α Subunit of Eukaryotic Initiation Factor 2 Is Required for Activation of NF-κB in Response to Diverse Cellular Stresses

Jiang, Hao-Yuan, Wek, Sheree A., McGrath, Barbara C., Scheuner, Donalyn, Kaufman, Randal J., Cavener, Douglas R., ...

Nuclear factor κB (NF-κB) serves to coordinate the transcription of genes in response to diverse environmental stresses. In this report we show that phosphorylation of the α subunit of eukaryotic...

Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

Cullinan, Sara B., Zhang, Donna, Hannink, Mark, Arvisais, Edward, Kaufman, Randal J., Diehl, J. Alan

Activation of PERK following the accumulation of unfolded proteins in the endoplasmic reticulum (ER) promotes translation inhibition and cell cycle arrest. PERK function is essential for cell...

Potential role of PKR in double-stranded RNA-induced macrophage activation

Maggi, Leonard B., Heitmeier, Monique R., Scheuner, Donalyn, Kaufman, Randal J., Buller, R.Mark L., Corbett, John A.

In this study, the role of the double-stranded (ds) RNA-dependent protein kinase (PKR) in macrophage activation was examined. dsRNA [polyinosinic:polycytidylic acid (poly IC)]-stimulated inducible...

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

Tirasophon, Witoon, Welihinda, Ajith A., Kaufman, Randal J.

Eukaryotes respond to the presence of unfolded protein in the endoplasmic reticulum (ER) by up-regulating the transcription of genes encoding ER protein chaperones, such as BiP. We have isolated a...

The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response

Tirasophon, Witoon, Lee, Kyungho, Callaghan, Brian, Welihinda, Ajith, Kaufman, Randal J.

The unfolded protein response (UPR) is a signal transduction pathway that is activated by the accumulation of unfolded proteins in the endoplasmic reticulum (ER). In Saccharomyces cerevisiae the ER...

The unfolded protein response represses nitrogen-starvation induced developmental differentiation in yeast

Schröder, Martin, Chang, Jason S., Kaufman, Randal J.

Diploid budding yeast exhibits two developmental programs in response to nitrogen starvation, pseudohyphal growth, and sporulation. Here we show that both programs are repressed by activation of the...

The unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylase

Schröder, Martin, Clark, Robert, Liu, Chuan Yin, Kaufman, Randal J

In Saccharomyces cerevisiae, splicing of HAC1 mRNA is initiated in response to the accumulation of unfolded proteins in the endoplasmic reticulum by the transmembrane kinase-endoribonuclease Ire1p....

Nck-dependent Activation of Extracellular Signal-regulated Kinase-1 and Regulation of Cell Survival during Endoplasmic Reticulum StressD⃞

Nguyên, Duc Thang, Kebache, Sem, Fazel, Ali, Wong, Hetty N., Jenna, Sarah, Emadali, Anouk, ...

In response to stress, the endoplasmic reticulum (ER) signaling machinery triggers the inhibition of protein synthesis and up-regulation of genes whose products are involved in protein folding, cell...

Translational Repression Mediates Activation of Nuclear Factor Kappa B by Phosphorylated Translation Initiation Factor 2

Deng, Jing, Lu, Phoebe D., Zhang, Yuhong, Scheuner, Donalyn, Kaufman, Randal J., Sonenberg, Nahum, ...

Numerous stressful conditions activate kinases that phosphorylate the alpha subunit of translation initiation factor 2 (eIF2α), thus attenuating mRNA translation and activating a gene expression...

The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis

Zhang, Kezhong, Wong, Hetty N., Song, Benbo, Miller, Corey N., Scheuner, Donalyn, Kaufman, Randal J.

B lymphocyte differentiation is coordinated with the induction of high-level Ig secretion and expansion of the secretory pathway. Upon accumulation of unfolded proteins in the lumen of the ER, cells...

Importance of eIF2α Phosphorylation and Stress Granule Assembly in Alphavirus Translation Regulation

McInerney, Gerald M., Kedersha, Nancy L., Kaufman, Randal J., Anderson, Paul, Liljeström, Peter

Alphavirus infection results in the shutoff of host protein synthesis in favor of viral translation. Here, we show that during Semliki Forest virus (SFV) infection, the translation inhibition is...

Genetic Interactions Due to Constitutive and Inducible Gene Regulation Mediated by the Unfolded Protein Response in C. elegans

Shen, Xiaohua, Ellis, Ronald E, Sakaki, Kenjiro, Kaufman, Randal J

The unfolded protein response (UPR) is an adaptive signaling pathway utilized to sense and alleviate the stress of protein folding in the endoplasmic reticulum (ER). In mammals, the UPR is mediated...

Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2

Lu, Phoebe D, Jousse, Céline, Marciniak, Stefan J, Zhang, Yuhong, Novoa, Isabel, Scheuner, Donalyn, ...

Transient phosphorylation of the α-subunit of translation initiation factor 2 (eIF2α) represses translation and activates select gene expression under diverse stressful conditions. Defects in the...

ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth

Bi, Meixia, Naczki, Christine, Koritzinsky, Marianne, Fels, Diane, Blais, Jaime, Hu, Nianping, ...

Tumor cell adaptation to hypoxic stress is an important determinant of malignant progression. While much emphasis has been placed on the role of HIF-1 in this context, the role of additional...

Bioactive small molecules reveal antagonism between the integrated stress response and sterol-regulated gene expression

Harding, Heather P., Zhang, Yuhong, Khersonsky, Sonya, Marciniak, Stefan, Scheuner, Donalyn, Kaufman, Randal J., ...

Phosphorylation of translation initiation factor 2α (eIF2α ) coordinates a translational and transcriptional program known as the integrated stress response (ISR), which adapts cells to endoplasmic...

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

Lee, Kyungho, Tirasophon, Witoon, Shen, Xiaohua, Michalak, Marek, Prywes, Ron, Okada, Tetsuya, ...

All eukaryotic cells respond to the accumulation of unfolded proteins in the endoplasmic reticulum (ER) by signaling an adaptive pathway termed the unfolded protein response (UPR). In yeast, a type-I...

Autocrine Tumor Necrosis Factor Alpha Links Endoplasmic Reticulum Stress to the Membrane Death Receptor Pathway through IRE1α-Mediated NF-κB Activation and Down-Regulation of TRAF2 Expression

Hu, Ping, Han, Zhang, Couvillon, Anthony D., Kaufman, Randal J., Exton, John H.

NF-κB is critical for determining cellular sensitivity to apoptotic stimuli by regulating both mitochondrial and death receptor apoptotic pathways. The endoplasmic reticulum (ER) emerges as a new...

Reovirus Induces and Benefits from an Integrated Cellular Stress Response

Smith, Jennifer A., Schmechel, Stephen C., Raghavan, Arvind, Abelson, Michelle, Reilly, Cavan, Katze, Michael G., ...

Following infection with most reovirus strains, viral protein synthesis is robust, even when cellular translation is inhibited. To gain further insight into pathways that regulate translation in...

Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins

Rutkowski, D. Thomas, Arnold, Stacey M, Miller, Corey N, Wu, Jun, Li, Jack, Gunnison, Kathryn M, ...

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) activates a signaling cascade known as the unfolded protein response (UPR). Although activation of the UPR is well described,...

Inhibition of Ribosome Recruitment Induces Stress Granule Formation Independently of Eukaryotic Initiation Factor 2α Phosphorylation

Mazroui, Rachid, Sukarieh, Rami, Bordeleau, Marie-Eve, Kaufman, Randal J., Northcote, Peter, Tanaka, Junichi, ...

Cytoplasmic aggregates known as stress granules (SGs) arise as a consequence of cellular stress and contain stalled translation preinitiation complexes. These foci are thought to serve as sites of...

Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p

Welihinda, Ajith A., Tirasophon, Witoon, Green, Sarah R., Kaufman, Randal J.

In eukaryotic cells, accumulation of unfolded protein in the endoplasmic reticulum induces transcription of a family of genes encoding endoplasmic reticulum protein chaperones through a conserved...

Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa

Pipe, Steven W., Kaufman, Randal J.

Individuals with hemophilia A require frequent infusion of preparations of coagulation factor VIII. The activity of factor VIII (FVIII) as a cofactor for factor IXa in the coagulation cascade is...

Double-Stranded RNA-Activated Protein Kinase (PKR) Is Negatively Regulated by 60S Ribosomal Subunit Protein L18

Kumar, Kotlo U., Srivastava, Sri P., Kaufman, Randal J.

The double-stranded RNA (dsRNA)-activated protein kinase (PKR) provides a fundamental control step in the regulation of protein synthesis initiation through phosphorylation of the alpha subunit of...

Regulation of starvation- and virus-induced autophagy by the eIF2α kinase signaling pathway

Tallóczy, Zsolt, Jiang, Wenxia, Virgin, Herbert W., Leib, David A., Scheuner, Donalyn, Kaufman, Randal J., ...

The eIF2α kinases are a family of evolutionarily conserved serine/threonine kinases that regulate stress-induced translational arrest. Here, we demonstrate that the yeast eIF2α kinase, GCN2, the...

Protein Serine/Threonine Phosphatase Ptc2p Negatively Regulates the Unfolded-Protein Response by Dephosphorylating Ire1p Kinase

Welihinda, Ajith A., Tirasophon, Witoon, Green, Sarah R., Kaufman, Randal J.

Cells respond to the accumulation of unfolded proteins in the endoplasmic reticulum (ER) by increasing the transcription of the genes encoding ER-resident chaperone proteins. Ire1p is a transmembrane...

In Vivo Replication of an ICP34.5 Second-Site Suppressor Mutant following Corneal Infection Correlates with In Vitro Regulation of eIF2α Phosphorylation

Ward, Stephen L., Scheuner, Donalyn, Poppers, Jeremy, Kaufman, Randal J., Mohr, Ian, Leib, David A.

In animal models of herpes simplex virus type 1 (HSV-1) infection, ICP34.5-null viruses are avirulent and also fail to grow in a variety of cultured cells due to their inability to prevent...

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

Lee, Kyungho, Tirasophon, Witoon, Shen, Xiaohua, Michalak, Marek, Prywes, Ron, Okada, Tetsuya, ...

All eukaryotic cells respond to the accumulation of unfolded proteins in the endoplasmic reticulum (ER) by signaling an adaptive pathway termed the unfolded protein response (UPR). In yeast, a type-I...

Optimization of protease-inhibitor interactions by randomizing adventitious contacts

Komiyama, Tomoko, VanderLugt, Bryan, Fugère, Martin, Day, Robert, Kaufman, Randal J., Fuller, Robert S.

Polypeptide protease inhibitors are often found to inhibit targets with which they did not coevolve, as in the case of high-affinity inhibition of bacterial subtilisin by the leech inhibitor eglin c....

Phosphorylation of the α Subunit of Eukaryotic Initiation Factor 2 Is Required for Activation of NF-κB in Response to Diverse Cellular Stresses

Jiang, Hao-Yuan, Wek, Sheree A., McGrath, Barbara C., Scheuner, Donalyn, Kaufman, Randal J., Cavener, Douglas R., ...

Nuclear factor κB (NF-κB) serves to coordinate the transcription of genes in response to diverse environmental stresses. In this report we show that phosphorylation of the α subunit of eukaryotic...

Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

Cullinan, Sara B., Zhang, Donna, Hannink, Mark, Arvisais, Edward, Kaufman, Randal J., Diehl, J. Alan

Activation of PERK following the accumulation of unfolded proteins in the endoplasmic reticulum (ER) promotes translation inhibition and cell cycle arrest. PERK function is essential for cell...

Potential role of PKR in double-stranded RNA-induced macrophage activation

Maggi, Leonard B., Heitmeier, Monique R., Scheuner, Donalyn, Kaufman, Randal J., Buller, R.Mark L., Corbett, John A.

In this study, the role of the double-stranded (ds) RNA-dependent protein kinase (PKR) in macrophage activation was examined. dsRNA [polyinosinic:polycytidylic acid (poly IC)]-stimulated inducible...

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

Tirasophon, Witoon, Welihinda, Ajith A., Kaufman, Randal J.

Eukaryotes respond to the presence of unfolded protein in the endoplasmic reticulum (ER) by up-regulating the transcription of genes encoding ER protein chaperones, such as BiP. We have isolated a...

The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response

Tirasophon, Witoon, Lee, Kyungho, Callaghan, Brian, Welihinda, Ajith, Kaufman, Randal J.

The unfolded protein response (UPR) is a signal transduction pathway that is activated by the accumulation of unfolded proteins in the endoplasmic reticulum (ER). In Saccharomyces cerevisiae the ER...

The unfolded protein response represses nitrogen-starvation induced developmental differentiation in yeast

Schröder, Martin, Chang, Jason S., Kaufman, Randal J.

Diploid budding yeast exhibits two developmental programs in response to nitrogen starvation, pseudohyphal growth, and sporulation. Here we show that both programs are repressed by activation of the...

The unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylase

Schröder, Martin, Clark, Robert, Liu, Chuan Yin, Kaufman, Randal J

In Saccharomyces cerevisiae, splicing of HAC1 mRNA is initiated in response to the accumulation of unfolded proteins in the endoplasmic reticulum by the transmembrane kinase-endoribonuclease Ire1p....

Nck-dependent Activation of Extracellular Signal-regulated Kinase-1 and Regulation of Cell Survival during Endoplasmic Reticulum StressD⃞

Nguyên, Duc Thang, Kebache, Sem, Fazel, Ali, Wong, Hetty N., Jenna, Sarah, Emadali, Anouk, ...

In response to stress, the endoplasmic reticulum (ER) signaling machinery triggers the inhibition of protein synthesis and up-regulation of genes whose products are involved in protein folding, cell...

Translational Repression Mediates Activation of Nuclear Factor Kappa B by Phosphorylated Translation Initiation Factor 2

Deng, Jing, Lu, Phoebe D., Zhang, Yuhong, Scheuner, Donalyn, Kaufman, Randal J., Sonenberg, Nahum, ...

Numerous stressful conditions activate kinases that phosphorylate the alpha subunit of translation initiation factor 2 (eIF2α), thus attenuating mRNA translation and activating a gene expression...

The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis

Zhang, Kezhong, Wong, Hetty N., Song, Benbo, Miller, Corey N., Scheuner, Donalyn, Kaufman, Randal J.

B lymphocyte differentiation is coordinated with the induction of high-level Ig secretion and expansion of the secretory pathway. Upon accumulation of unfolded proteins in the lumen of the ER, cells...

Importance of eIF2α Phosphorylation and Stress Granule Assembly in Alphavirus Translation Regulation

McInerney, Gerald M., Kedersha, Nancy L., Kaufman, Randal J., Anderson, Paul, Liljeström, Peter

Alphavirus infection results in the shutoff of host protein synthesis in favor of viral translation. Here, we show that during Semliki Forest virus (SFV) infection, the translation inhibition is...

Genetic Interactions Due to Constitutive and Inducible Gene Regulation Mediated by the Unfolded Protein Response in C. elegans

Shen, Xiaohua, Ellis, Ronald E, Sakaki, Kenjiro, Kaufman, Randal J

The unfolded protein response (UPR) is an adaptive signaling pathway utilized to sense and alleviate the stress of protein folding in the endoplasmic reticulum (ER). In mammals, the UPR is mediated...

Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2

Lu, Phoebe D, Jousse, Céline, Marciniak, Stefan J, Zhang, Yuhong, Novoa, Isabel, Scheuner, Donalyn, ...

Transient phosphorylation of the α-subunit of translation initiation factor 2 (eIF2α) represses translation and activates select gene expression under diverse stressful conditions. Defects in the...

ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth

Bi, Meixia, Naczki, Christine, Koritzinsky, Marianne, Fels, Diane, Blais, Jaime, Hu, Nianping, ...

Tumor cell adaptation to hypoxic stress is an important determinant of malignant progression. While much emphasis has been placed on the role of HIF-1 in this context, the role of additional...

Reovirus Induces and Benefits from an Integrated Cellular Stress Response

Smith, Jennifer A., Schmechel, Stephen C., Raghavan, Arvind, Abelson, Michelle, Reilly, Cavan, Katze, Michael G., ...

Following infection with most reovirus strains, viral protein synthesis is robust, even when cellular translation is inhibited. To gain further insight into pathways that regulate translation in...

Autocrine Tumor Necrosis Factor Alpha Links Endoplasmic Reticulum Stress to the Membrane Death Receptor Pathway through IRE1α-Mediated NF-κB Activation and Down-Regulation of TRAF2 Expression

Hu, Ping, Han, Zhang, Couvillon, Anthony D., Kaufman, Randal J., Exton, John H.

NF-κB is critical for determining cellular sensitivity to apoptotic stimuli by regulating both mitochondrial and death receptor apoptotic pathways. The endoplasmic reticulum (ER) emerges as a new...

Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins

Rutkowski, D. Thomas, Arnold, Stacey M, Miller, Corey N, Wu, Jun, Li, Jack, Gunnison, Kathryn M, ...

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) activates a signaling cascade known as the unfolded protein response (UPR). Although activation of the UPR is well described,...

Inhibition of Ribosome Recruitment Induces Stress Granule Formation Independently of Eukaryotic Initiation Factor 2α Phosphorylation

Mazroui, Rachid, Sukarieh, Rami, Bordeleau, Marie-Eve, Kaufman, Randal J., Northcote, Peter, Tanaka, Junichi, ...

Cytoplasmic aggregates known as stress granules (SGs) arise as a consequence of cellular stress and contain stalled translation preinitiation complexes. These foci are thought to serve as sites of...

Initiation of Protein Synthesis by Hepatitis C Virus Is Refractory to Reduced eIF2 · GTP · Met-tRNAiMet Ternary Complex Availability

Robert, Francis, Kapp, Lee D., Khan, Shakila N., Acker, Michael G., Kolitz, Sarah, Kazemi, Shirin, ...

A cornerstone of the antiviral interferon response is phosphorylation of eukaryotic initiation factor (eIF)2α. This limits the availability of eIF2·GTP·Met-tRNAiMet ternary complexes, reduces...

Gene expression during acute and prolonged hypoxia is regulated by distinct mechanisms of translational control

Koritzinsky, Marianne, Magagnin, Michaël G, Van Den Beucken, Twan, Seigneuric, Renaud, Savelkouls, Kim, Dostie, Josée, ...

Hypoxia has recently been shown to activate the endoplasmic reticulum kinase PERK, leading to phosphorylation of eIF2α and inhibition of mRNA translation initiation. Using a quantitative assay, we...

The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response

Zhou, Jiahai, Liu, Chuan Yin, Back, Sung Hoon, Clark, Robert L., Peisach, Daniel, Xu, Zhaohui, ...

The unfolded protein response (UPR) is an evolutionarily conserved mechanism by which all eukaryotic cells adapt to the accumulation of unfolded proteins in the endoplasmic reticulum (ER)....

Mechanisms of β-Cell Death in Response to Double-Stranded (ds) RNA and Interferon-γ : dsRNA-Dependent Protein Kinase Apoptosis and Nitric Oxide-Dependent Necrosis

Scarim, Anna L., Arnush, Marc, Blair, Libby A., Concepcion, Josephine, Heitmeier, Monique R., Scheuner, Donalyn, ...

Viral infection is one environmental factor that has been implicated as a precipitating event that may initiate β-cell damage during the development of diabetes. This study examines the mechanisms...

Combined deficiency of factor V and factor VIII is due to mutations in either LMAN1 or MCFD2

Zhang, Bin, McGee, Beth, Yamaoka, Jennifer S., Guglielmone, Hugo, Downes, Katharine A., Minoldo, Salvador, ...

Mutations in LMAN1 (ERGIC-53) or MCFD2 cause combined deficiency of factor V and factor VIII (F5F8D). LMAN1 and MCFD2 form a protein complex that functions as a cargo receptor ferrying FV and FVIII...

Inhibition of the Ubiquitin-Proteasome System Induces Stress Granule Formation

Mazroui, Rachid, Di Marco, Sergio, Kaufman, Randal J., Gallouzi, Imed-Eddine

The inhibition of the ubiquitin-dependent proteasome system (UPS) via specific drugs is one type of approach used to combat cancer. Although it has been suggested that UPS inhibition prevents the...

The Role of p58IPK in Protecting the Stressed Endoplasmic Reticulum

Rutkowski, D. Thomas, Kang, Sang-Wook, Goodman, Alan G., Garrison, Jennifer L., Taunton, Jack, Katze, Michael G., ...

The preemptive quality control (pQC) pathway protects cells from acute endoplasmic reticulum (ER) stress by attenuating translocation of nascent proteins despite their targeting to translocons at the...

Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation

Oda, Yukako, Okada, Tetsuya, Yoshida, Hiderou, Kaufman, Randal J., Nagata, Kazuhiro, Mori, Kazutoshi

Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded or degraded to maintain the homeostasis of the ER. Components of both productive folding and ER-associated...

Translation attenuation by PERK balances ER glycoprotein synthesis with lipid-linked oligosaccharide flux

Shang, Jie, Gao, Ningguo, Kaufman, Randal J., Ron, David, Harding, Heather P., Lehrman, Mark A.

Endoplasmic reticulum (ER) homeostasis requires transfer and subsequent processing of the glycan Glc3Man9GlcNAc2 (G3M9Gn2) from the lipid-linked oligosaccharide (LLO)...

Stress granules and processing bodies are dynamically linked sites of mRNP remodeling

Kedersha, Nancy, Stoecklin, Georg, Ayodele, Maranatha, Yacono, Patrick, Lykke-Andersen, Jens, Fritzler, Marvin J., ...

Stress granules (SGs) are cytoplasmic aggregates of stalled translational preinitiation complexes that accumulate during stress. GW bodies/processing bodies (PBs) are distinct cytoplasmic sites of...

Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradation

Nagasawa, Koji, Higashi, Toshio, Hosokawa, Nobuko, Kaufman, Randal J, Nagata, Kazuhiro

The mammalian translocon-associated protein (TRAP) complex comprises four transmembrane protein subunits in the endoplasmic reticulum. The complex associates with the Sec61 translocon, although its...

Fatal hemorrhage in mice lacking γ-glutamyl carboxylase

Zhu, Aihua, Sun, Hongmin, Raymond, Richard M., Furie, Barbara C., Furie, Bruce, Bronstein, Mila, ...

The carboxylation of glutamic acid residues to γ-carboxyglutamic acid (Gla) by the vitamin K–dependent γ-glutamyl carboxylase (γ-carboxylase) is an essential posttranslational modification...

An efficient in vitro translation system from mammalian cells lacking the translational inhibition caused by eIF2 phosphorylation

Zeenko, Vladimir V., Wang, Chuanping, Majumder, Mithu, Komar, Anton A., Snider, Martin D., Merrick, William C., ...

In vitro translation systems are used to investigate translational mechanisms and to synthesize proteins for characterization. Most available mammalian cell-free systems have reduced efficiency due...

Chop deletion reduces oxidative stress, improves β cell function, and promotes cell survival in multiple mouse models of diabetes

Song, Benbo, Scheuner, Donalyn, Ron, David, Pennathur, Subramaniam, Kaufman, Randal J.

The progression from insulin resistance to type 2 diabetes is caused by the failure of pancreatic β cells to produce sufficient levels of insulin to meet the metabolic demand. Recent studies...

MEK Signaling Is Required for Phosphorylation of eIF2α following Amino Acid Limitation of HepG2 Human Hepatoma Cells*

Thiaville, Michelle M., Pan, Yuan-Xiang, Gjymishka, Altin, Zhong, Can, Kaufman, Randal J., Kilberg, Michael S.

The mammalian amino acid response (AAR) pathway is up-regulated by protein or amino acid depletion. This pathway involves detection of uncharged tRNA by the GCN2 kinase, phosphorylation of the...

The Unfolded Protein Response: A Pathway That Links Insulin Demand with β-Cell Failure and Diabetes

Scheuner, Donalyn, Kaufman, Randal J.

The endoplasmic reticulum (ER) is the entry site into the secretory pathway for newly synthesized proteins destined for the cell surface or released into the extracellular milieu. The study of...

Antioxidants reduce endoplasmic reticulum stress and improve protein secretion

Malhotra, Jyoti D., Miao, Hongzhi, Zhang, Kezhong, Wolfson, Anna, Pennathur, Subramaniam, Pipe, Steven W., ...

Protein misfolding in the endoplasmic reticulum (ER) contributes to the pathogenesis of many diseases. Although oxidative stress can disrupt protein folding, how protein misfolding and oxidative...

Protein Kinase Cθ Is Required for Autophagy in Response to Stress in the Endoplasmic Reticulum*S⃞

Sakaki, Kenjiro, Wu, Jun, Kaufman, Randal J.

Autophagy is an evolutionally conserved process for the bulk degradation of cytoplasmic proteins and organelles. Recent observations indicate that autophagy is induced in response to cellular insults...

Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS

Wang, Jiou, Farr, George W., Zeiss, Caroline J., Rodriguez-Gil, Diego J., Wilson, Jean H., Furtak, Krystyna, ...

Recent studies suggest that superoxide dismutase 1 (SOD1)-linked amyotrophic lateral sclerosis results from destabilization and misfolding of mutant forms of this abundant cytosolic enzyme. Here, we...

Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2α) dephosphorylation in mammalian development

Harding, Heather P., Zhang, Yuhong, Scheuner, Donalyn, Chen, Jane-Jane, Kaufman, Randal J., Ron, David

Diverse cellular stress responses are linked to phosphorylation of serine 51 on the alpha subunit of translation initiation factor 2. The resultant attenuation of protein synthesis and activation of...

Uncoupling Stress Granule Assembly and Translation Initiation Inhibition

Mokas, Sophie, Mills, John R., Garreau, Cristina, Fournier, Marie-Josée, Robert, Francis, Arya, Prabhat, ...

Cytoplasmic stress granules (SGs) are specialized regulatory sites of mRNA translation that form under different stress conditions known to inhibit translation initiation. The formation of SG occurs...

Novel Function of PERK as a Mediator of Force-induced Apoptosis*

Mak, Baldwin C., Wang, Qin, Laschinger, Carol, Lee, Wilson, Ron, David, Harding, Heather P., ...

Induction of apoptosis by tensile forces is an important determinant of connective tissue destruction in osteoarthritis and periodontal diseases. We examined the role of molecular components of the...

ATF6α induces XBP1-independent expansion of the endoplasmic reticulum

Bommiasamy, Hemamalini, Back, Sung Hoon, Fagone, Paolo, Lee, Kyungho, Meshinchi, Sasha, Vink, Elizabeth, ...

A link exists between endoplasmic reticulum (ER) biogenesis and the unfolded protein response (UPR), a complex set of signaling mechanisms triggered by increased demands on the protein folding...