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...
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...
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...
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...
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...