Michael K. Rosen

Publication List Details

Period

1998 - 2009

Number

16

Co-Authors

Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation (2009)

Vingadassalom, Didier F., Kazlauskas, Arunas, Skehan, Brian M., Cheng, Hui-Chun, Magoun, Loranne, Robbins, Douglas, ...

Enterohemorrhagic Escherichia coli O157:H7 translocates 2 effectors to trigger localized actin assembly in mammalian cells, resulting in filamentous actin "pedestals." One effector, the...

Hierarchical regulation of WASP/WAVE proteins (2008)

Padrick, Shae B., Cheng, Hui-Chun, Ismail, Ayman M., Panchal, Sanjay C., Doolittle, Lynda K., Kim, Soyeon, ...

Members of the Wiskott-Aldrich syndrome protein (WASP) family control actin dynamics in eukaryotic cells by stimulating the actin nucleating activity of the Arp2/3 complex. The prevailing paradigm...

Repetitive N-WASP-binding elements of the enterohemorrhagic Escherichia coli effector EspF(U) synergistically activate actin assembly (2008)

Campellone, Kenneth Geno, Cheng, Hui-Chun, Robbins, Douglas, Siripala, Anosha D., McGhie, Emma J., Hayward, Richard D., ...

Enterohemorrhagic Escherichia coli (EHEC) generate F-actin-rich adhesion pedestals by delivering effector proteins into mammalian cells. These effectors include the translocated receptor Tir, along...

Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U) (2008)

Cheng, Hui-Chun, Skehan, Brian M., Campellone, Kenneth Geno, Leong, John M., Rosen, Michael K.

During infection, enterohaemorrhagic Escherichia coli (EHEC) takes over the actin cytoskeleton of eukaryotic cells by injecting the EspF(U) protein into the host cytoplasm. EspF(U) controls actin by...

Structure Elucidation of the Rho-GTPhase Activating DH-Homology Domain (1998)

Aghazadeh, Behzad, Rosen, Michael K.

Rho-family of small GTPases transduce signals from receptors to modulate various physiological responses including cytoskeletal reorganization leading to changes in cell shape and motility,...

Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6

Garrard, Sarah M., Capaldo, Christopher T., Gao, Lin, Rosen, Michael K., Macara, Ian G., Tomchick, Diana R.

Cdc42 is a small GTPase that is required for cell polarity establishment in eukaryotes as diverse as budding yeast and mammals. Par6 is also implicated in metazoan cell polarity establishment and...

The nucleotide switch in Cdc42 modulates coupling between the GTPase-binding and allosteric equilibria of Wiskott–Aldrich syndrome protein

Leung, Daisy W., Rosen, Michael K.

The GTP/GDP nucleotide switch in Ras superfamily GTPases generally involves differential affinity toward downstream effectors, with the GTP-bound state having a higher affinity for effector than the...

Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6

Garrard, Sarah M., Capaldo, Christopher T., Gao, Lin, Rosen, Michael K., Macara, Ian G., Tomchick, Diana R.

Cdc42 is a small GTPase that is required for cell polarity establishment in eukaryotes as diverse as budding yeast and mammals. Par6 is also implicated in metazoan cell polarity establishment and...

The nucleotide switch in Cdc42 modulates coupling between the GTPase-binding and allosteric equilibria of Wiskott–Aldrich syndrome protein

Leung, Daisy W., Rosen, Michael K.

The GTP/GDP nucleotide switch in Ras superfamily GTPases generally involves differential affinity toward downstream effectors, with the GTP-bound state having a higher affinity for effector than the...

Signal transduction pathway of TonB-dependent transporters

Ferguson, Andrew D., Amezcua, Carlos A., Halabi, Najeeb M., Chelliah, Yogarany, Rosen, Michael K., Ranganathan, Rama, ...

Transcription of the ferric citrate import system is regulated by ferric citrate binding to the outer membrane transporter FecA. A signal indicating transporter occupancy is relayed across the outer...

Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLα and mDia1

Seth, Abhinav, Otomo, Chinatsu, Rosen, Michael K.

Diaphanous-related formins (DRFs) are key regulators of actin cytoskeletal dynamics whose in vitro actin assembly activities are thought to be regulated by autoinhibition. However, the in vivo...

A novel mechanism of actin filament processive capping by formin: solution of the rotation paradox

Shemesh, Tom, Otomo, Takanori, Rosen, Michael K., Bershadsky, Alexander D., Kozlov, Michael M.

The FH2 domains of formin family proteins act as processive cappers of actin filaments. Previously suggested stair-stepping mechanisms of processive capping imply that a formin cap rotates...

Arp2/3-independent assembly of actin by Vibrio type III effector VopL

Liverman, Amy D. B., Cheng, Hui-Chun, Trosky, Jennifer E., Leung, Daisy W., Yarbrough, Melanie L., Burdette, Dara L., ...

Microbial pathogens use a variety of mechanisms to disrupt the actin cytoskeleton during infection. Vibrio parahaemolyticus (V. para) is a Gram-negative bacterium that causes gastroenteritis, and new...

Repetitive N-WASP–Binding Elements of the Enterohemorrhagic Escherichia coli Effector EspFU Synergistically Activate Actin Assembly

Campellone, Kenneth G., Cheng, Hui-Chun, Robbins, Douglas, Siripala, Anosha D., McGhie, Emma J., Hayward, Richard D., ...

Enterohemorrhagic Escherichia coli (EHEC) generate F-actin–rich adhesion pedestals by delivering effector proteins into mammalian cells. These effectors include the translocated receptor Tir, along...

Genetically encoded photoswitching of actin assembly through the Cdc42-WASP-Arp2/3 complex pathway

Leung, Daisy W., Otomo, Chinatsu, Chory, Joanne, Rosen, Michael K.

General methods to engineer genetically encoded, reversible, light-mediated control over protein function would be useful in many areas of biomedical research and technology. We describe a system...

Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspFU during pedestal formation

Vingadassalom, Didier, Kazlauskas, Arunas, Skehan, Brian, Cheng, Hui-Chun, Magoun, Loranne, Robbins, Douglas, ...

Enterohemorrhagic Escherichia coli O157:H7 translocates 2 effectors to trigger localized actin assembly in mammalian cells, resulting in filamentous actin “pedestals.” One effector, the...