Enno Hartmann

Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP (2008)

Linder, Bastian, Plöttner, Oliver, Kroiss, Matthias, Hartmann, Enno, Laggerbauer, Bernhard, Meister, Gunter, ...

Tudor domains are widespread among proteins involved in RNA metabolism, but only in a few cases their cellular function has been analyzed in detail. Here, we report on the characterization of the...

Dissertation zur Erlangung des akademischen Grades (2005)

Christoph Hammerschmidt, Aus Göttingen, Beda Christoph Hammerschmidt, Dekan Prof, Dr. Enno Hartmann, ...

I would like to thank my colleague Dr. Martin Kempa and my supervisor Prof. Dr. Volker Linnemann for the excellent cooperation, many helpful suggestions, and reviews. Special acknowledgments go to...

Sec61p is Adjacent to Nascent Type I and Type II Signal-Anchor Proteins during Their Membrane Insertion (1993)

High, Stephen, Andersen, Soren S. L., Görlich, Dirk, Hartmann, Enno, Prehn, Siegfried, Rapoport, Tom A., ...

We have identified membrane components which are adjacent to type I and type II signal-anchor proteins during their insertion into the membrane of the ER. Using two different cross-linking approaches...

Site-specific Photocross-linking Reveals That SecGlp and TRAM Contact Different Regions of a Membrane-inserted Signal Sequence (1993)

High, Stephen, Martoglio, Bruno, Görlich, Dirk, Andersen, Soren S. L., Ashford, Anthony J., Giner, Angelika, ...

A chemically charged amber suppressor tRNA was used to introduce the photoactivatable amino acid (Tmd)Phe at a selected position within the signal sequence of the secretory protein preprolactin. This...

The Signal Sequence Receptor Has a Second Subunit and IsPart of a Translocation Complex in the Endoplasmic Reticulum as Probed by Bifunctional Reagents (1990)

Görlich, Dirk, Prehn, Siegfried, Hartmann, Enno, Herz, Joachim, Otto, Albrecht, Kraft, Regine, ...

Bifunctional cross-linking reagents were used to probe the protein environment in the ER membrane of the signal sequence receptor (SSR), a 34-kD integral membrane glycoprotein (Wiedmann, M., T. V....

Structure and biosynthesis of the signal-sequence receptor (1990)

Prehn, Siegfried, Herz, Joachim, Hartmann, Enno, Kurzchalia, Teymuras V., Frank, Rainer, Römisch, Karin, ...

The signal-sequence receptor (SSR) has previously been shown to be a component of the environment which nascent polypeptides meet on passage through the endoplasmic reticulum (ER) membrane. We report...

Evidence for Distinct Substrate Specificities of Importin α Family Members in Nuclear Protein Import

Köhler, Matthias, Speck, Christian, Christiansen, Marret, Bischoff, F. Ralf, Prehn, Siegfried, Haller, Hermann, ...

Importin α plays a pivotal role in the classical nuclear protein import pathway. Importin α shuttles between nucleus and cytoplasm, binds nuclear localization signal-bearing proteins, and functions...

Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains

Jäkel, Stefan, Mingot, José-Manuel, Schwarzmaier, Petra, Hartmann, Enno, Görlich, Dirk

Many nuclear transport pathways are mediated by importin β-related transport receptors. Here, we identify human importin (Imp) 4b as well as mouse Imp4a, Imp9a and Imp9b as novel family members....

SMNrp is an essential pre-mRNA splicing factor required for the formation of the mature spliceosome

Meister, Gunter, Hannus, Stefan, Plöttner, Oliver, Baars, Tonie, Hartmann, Enno, Fakan, Stanislav, ...

SMNrp, also termed SPF30, has recently been identified in spliceosomes assembled in vitro. We have functionally characterized this protein and show that it is an essential splicing factor. We show...

Importin 13: a novel mediator of nuclear import and export

Mingot, José-Manuel, Kostka, Susanne, Kraft, Regine, Hartmann, Enno, Görlich, Dirk

Importin β-related receptors mediate translocation through nuclear pore complexes. Co-operation with the RanGTPase system allows them to bind and subsequently release their substrates on opposite...

Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm

Bohnsack, Markus T., Regener, Kathrin, Schwappach, Blanche, Saffrich, Rainer, Paraskeva, Efrosyni, Hartmann, Enno, ...

Importin β-type transport receptors mediate the vast majority of transport pathways between cell nucleus and cytoplasm. We identify here the translation elongation factor 1A (eEF1A) as the...

Prokaryotic Utilization of the Twin-Arginine Translocation Pathway: a Genomic Survey

Dilks, Kieran, Rose, R. Wesley, Hartmann, Enno, Pohlschröder, Mechthild

The twin-arginine translocation (Tat) pathway, which has been identified in plant chloroplasts and prokaryotes, allows for the secretion of folded proteins. However, the extent to which this pathway...

Use1p is a yeast SNARE protein required for retrograde traffic to the ER

Dilcher, Meik, Veith, Beate, Chidambaram, Subbulakshmi, Hartmann, Enno, Schmitt, Hans Dieter, Fischer Von Mollard, Gabriele

SNAREs on transport vesicles and target membranes are required for vesicle targeting and fusion. Here we describe a novel yeast protein with a typical SNARE motif but with low overall amino acid...

Exportin 6: a novel nuclear export receptor that is specific for profilin·actin complexes

Stüven, Theis, Hartmann, Enno, Görlich, Dirk

Active macromolecular transport between the nucleus and cytoplasm proceeds through nuclear pore complexes and is mostly mediated by transport receptors of the importin β-superfamily. Here we...

Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA

Prinz, Anke, Behrens, Christina, Rapoport, Tom A., Hartmann, Enno, Kalies, Kai-Uwe

During early stages of cotranslational protein translocation across the endoplasmic reticulum (ER) membrane the ribosome is targeted to the heterotrimeric Sec61p complex, the major component of the...

Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes

Lipowsky, Gerd, Bischoff, F.Ralf, Schwarzmaier, Petra, Kraft, Regine, Kostka, Susanne, Hartmann, Enno, ...

Transport receptors of the importin β superfamily account for many of the nuclear import and export events in eukaryotic cells. They mediate translocation through nuclear pore complexes, shuttle...

In Vivo Analysis of Importin α Proteins Reveals Cellular Proliferation Inhibition and Substrate Specificity

Quensel, Christina, Friedrich, Beate, Sommer, Thomas, Hartmann, Enno, Kohler, Matthias

The “classical” nuclear import pathway depends on importins α and β. Humans have only one importin β, while six α importins have been described. Whether or not distinct α importins are...

Deletion of SERP1/RAMP4, a Component of the Endoplasmic Reticulum (ER) Translocation Sites, Leads to ER Stress

Hori, Osamu, Miyazaki, Mayuki, Tamatani, Takashi, Ozawa, Kentaro, Takano, Katsura, Okabe, Masaru, ...

Stress-associated endoplasmic reticulum (ER) protein 1 (SERP1), also known as ribosome-associated membrane protein 4 (RAMP4), is a Sec61-associated polypeptide that is induced by ER stress....

Evidence for Distinct Substrate Specificities of Importin α Family Members in Nuclear Protein Import

Köhler, Matthias, Speck, Christian, Christiansen, Marret, Bischoff, F. Ralf, Prehn, Siegfried, Haller, Hermann, ...

Importin α plays a pivotal role in the classical nuclear protein import pathway. Importin α shuttles between nucleus and cytoplasm, binds nuclear localization signal-bearing proteins, and functions...

Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains

Jäkel, Stefan, Mingot, José-Manuel, Schwarzmaier, Petra, Hartmann, Enno, Görlich, Dirk

Many nuclear transport pathways are mediated by importin β-related transport receptors. Here, we identify human importin (Imp) 4b as well as mouse Imp4a, Imp9a and Imp9b as novel family members....

SMNrp is an essential pre-mRNA splicing factor required for the formation of the mature spliceosome

Meister, Gunter, Hannus, Stefan, Plöttner, Oliver, Baars, Tonie, Hartmann, Enno, Fakan, Stanislav, ...

SMNrp, also termed SPF30, has recently been identified in spliceosomes assembled in vitro. We have functionally characterized this protein and show that it is an essential splicing factor. We show...

Importin 13: a novel mediator of nuclear import and export

Mingot, José-Manuel, Kostka, Susanne, Kraft, Regine, Hartmann, Enno, Görlich, Dirk

Importin β-related receptors mediate translocation through nuclear pore complexes. Co-operation with the RanGTPase system allows them to bind and subsequently release their substrates on opposite...

Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm

Bohnsack, Markus T., Regener, Kathrin, Schwappach, Blanche, Saffrich, Rainer, Paraskeva, Efrosyni, Hartmann, Enno, ...

Importin β-type transport receptors mediate the vast majority of transport pathways between cell nucleus and cytoplasm. We identify here the translation elongation factor 1A (eEF1A) as the...

Prokaryotic Utilization of the Twin-Arginine Translocation Pathway: a Genomic Survey

Dilks, Kieran, Rose, R. Wesley, Hartmann, Enno, Pohlschröder, Mechthild

The twin-arginine translocation (Tat) pathway, which has been identified in plant chloroplasts and prokaryotes, allows for the secretion of folded proteins. However, the extent to which this pathway...

Use1p is a yeast SNARE protein required for retrograde traffic to the ER

Dilcher, Meik, Veith, Beate, Chidambaram, Subbulakshmi, Hartmann, Enno, Schmitt, Hans Dieter, Fischer Von Mollard, Gabriele

SNAREs on transport vesicles and target membranes are required for vesicle targeting and fusion. Here we describe a novel yeast protein with a typical SNARE motif but with low overall amino acid...

Exportin 6: a novel nuclear export receptor that is specific for profilin·actin complexes

Stüven, Theis, Hartmann, Enno, Görlich, Dirk

Active macromolecular transport between the nucleus and cytoplasm proceeds through nuclear pore complexes and is mostly mediated by transport receptors of the importin β-superfamily. Here we...

Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA

Prinz, Anke, Behrens, Christina, Rapoport, Tom A., Hartmann, Enno, Kalies, Kai-Uwe

During early stages of cotranslational protein translocation across the endoplasmic reticulum (ER) membrane the ribosome is targeted to the heterotrimeric Sec61p complex, the major component of the...

Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes

Lipowsky, Gerd, Bischoff, F.Ralf, Schwarzmaier, Petra, Kraft, Regine, Kostka, Susanne, Hartmann, Enno, ...

Transport receptors of the importin β superfamily account for many of the nuclear import and export events in eukaryotic cells. They mediate translocation through nuclear pore complexes, shuttle...

In Vivo Analysis of Importin α Proteins Reveals Cellular Proliferation Inhibition and Substrate Specificity

Quensel, Christina, Friedrich, Beate, Sommer, Thomas, Hartmann, Enno, Kohler, Matthias

The “classical” nuclear import pathway depends on importins α and β. Humans have only one importin β, while six α importins have been described. Whether or not distinct α importins are...

Deletion of SERP1/RAMP4, a Component of the Endoplasmic Reticulum (ER) Translocation Sites, Leads to ER Stress

Hori, Osamu, Miyazaki, Mayuki, Tamatani, Takashi, Ozawa, Kentaro, Takano, Katsura, Okabe, Masaru, ...

Stress-associated endoplasmic reticulum (ER) protein 1 (SERP1), also known as ribosome-associated membrane protein 4 (RAMP4), is a Sec61-associated polypeptide that is induced by ER stress....

Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi

Trautwein, Mark, Schindler, Christina, Gauss, Robert, Dengjel, Jörn, Hartmann, Enno, Spang, Anne

In Saccharomyces cerevisiae, the synthesis of chitin is temporally and spatially regulated through the transport of Chs3p (chitin synthase III) to the plasma membrane in the bud neck region. Traffic...

Nuclear Localization Signal and Protein Context both Mediate Importin α Specificity of Nuclear Import Substrates▿

Friedrich, Beate, Quensel, Christina, Sommer, Thomas, Hartmann, Enno, Köhler, Matthias

The “classical” nuclear protein import pathway depends on importin α and importin β. Importin α binds nuclear localization signal (NLS)-bearing proteins and functions as an adapter to access...

NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes

Stavru, Fabrizia, Hülsmann, Bastian B., Spang, Anne, Hartmann, Enno, Cordes, Volker C., Görlich, Dirk

POM121 and gp210 were, until this point, the only known membrane-integral nucleoporins (Nups) of vertebrates and, thus, the only candidate anchors for nuclear pore complexes (NPCs) within the nuclear...

The β Subunit of the Sec61 Complex Facilitates Cotranslational Protein Transport and Interacts with the Signal Peptidase during Translocation

Kalies, Kai-Uwe, Rapoport, Tom A., Hartmann, Enno

The Sec61 complex is the central component of the protein translocation apparatus of the ER membrane. We have addressed the role of the β subunit (Sec61β) during cotranslational protein...

CRM1-mediated Recycling of Snurportin 1 to the Cytoplasm

Paraskeva, Efrosyni, Izaurralde, Elisa, Bischoff, F. Ralf, Huber, Jochen, Kutay, Ulrike, Hartmann, Enno, ...

Importin β is a major mediator of import into the cell nucleus. Importin β binds cargo molecules either directly or via two types of adapter molecules, importin α, for import of proteins with a...

A Novel Class of RanGTP Binding Proteins

Görlich, Dirk, Dabrowski, Marylena, Bischoff, F. Ralf, Kutay, Ulrike, Bork, Peer, Hartmann, Enno, ...

The importin-α/β complex and the GTPase Ran mediate nuclear import of proteins with a classical nuclear localization signal. Although Ran has been implicated also in a variety of other processes,...

Stress-Associated Endoplasmic Reticulum Protein 1 (Serp1)/Ribosome-Associated Membrane Protein 4 (Ramp4) Stabilizes Membrane Proteins during Stress and Facilitates Subsequent Glycosylation

Yamaguchi, Atsushi, Hori, Osamu, Stern, David M., Hartmann, Enno, Ogawa, Satoshi, Tohyama, Masaya

Application of differential display to cultured rat astrocytes subjected to hypoxia allowed cloning of a novel cDNA, termed stress-associated endoplasmic reticulum protein 1 (SERP1). Expression of...