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10.4161/sgtp.29513 http://scihub22266oqcxt.onion/10.4161/sgtp.29513 C4111664!4111664!24914801     free     free     free       Small+GTPases 2014 ; 5 (ä): ä Nephropedia Template TP {{tp|p=24914801|t=2014. Formins as effector proteins of Rho GTPases |pdf=|usr=}}{{24914801}} gab.com Text Formins as effector proteins of Rho GTPases JO: Small GTPases http://www.kidney.de/pget.php?&tw=1&pmid=24914801 #FOAvip Formin proteins were recognized as effectors of Rho GTPases some 15 years ago. They contribute to different cellular actin cytoskeleton structures by their ability to polymerize straight actin filaments at the barbed end. While not all formins necessarily interact with Rho GTPases, a subgroup of mammalian formins, termed Diaphanous-related formins or DRFs, were shown to be activated by small GTPases of the Rho superfamily. DRFs are autoinhibited in the resting state by an N- to C-terminal interaction that renders the central actin polymerization domain inactive. Upon the interaction with a GTP-bound Rho, Rac, or Cdc42 GTPase, the C-terminal autoregulation domain is displaced from its N-terminal recognition site and the formin becomes active to polymerize actin filaments. In this review we discuss the current knowledge on the structure, activation, and function of formin-GTPase interactions for the mammalian formin families Dia, Daam, FMNL, and FHOD. We describe both direct and indirect interactions of formins with GTPases, which lead to formin activation and cytoskeletal rearrangements. The multifaceted function of formins as effector proteins of Rho GTPases thus reflects the diversity of the actin cytoskeleton in cells. Twit Text FOAVip Formins as effector proteins of Rho GTPases ????Small GTPases http://www.kidney.de/pget.php?&tw=1&pmid=24914801 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24914801 #FOAvip English Wikipedia <ref>{{Cite pmid|24914801}}</ref> Formins as effector proteins of Rho GTPases #MMPMID24914801 Kühn S; Geyer M Small GTPases 2014[]; 5 (ä): ä PMID24914801show ga Formin proteins were recognized as effectors of Rho GTPases some 15 years ago. They contribute to different cellular actin cytoskeleton structures by their ability to polymerize straight actin filaments at the barbed end. While not all formins necessarily interact with Rho GTPases, a subgroup of mammalian formins, termed Diaphanous-related formins or DRFs, were shown to be activated by small GTPases of the Rho superfamily. DRFs are autoinhibited in the resting state by an N- to C-terminal interaction that renders the central actin polymerization domain inactive. Upon the interaction with a GTP-bound Rho, Rac, or Cdc42 GTPase, the C-terminal autoregulation domain is displaced from its N-terminal recognition site and the formin becomes active to polymerize actin filaments. In this review we discuss the current knowledge on the structure, activation, and function of formin-GTPase interactions for the mammalian formin families Dia, Daam, FMNL, and FHOD. We describe both direct and indirect interactions of formins with GTPases, which lead to formin activation and cytoskeletal rearrangements. The multifaceted function of formins as effector proteins of Rho GTPases thus reflects the diversity of the actin cytoskeleton in cells. äFormins as effector proteins of Rho GTPases (epmc).pdf DeepDyve Pubget Overpricing