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• W2085751189 abstract "Semaphorins and their receptors, plexins, are widely expressed in embryonic and adult tissues. In general, their functions are poorly characterized, but in neurons they provide essential attractive and repulsive cues that are necessary for axon guidance [1Maestrini E. Tamagnone L. Longati P. Cremona O. Gulisano M. Bione S. et al.A family of transmembrane proteins with homology to the MET-hepatocyte growth factor receptor.Proc Natl Acad Sci. 1996; 93: 674-678Crossref PubMed Scopus (145) Google Scholar, 2Tamagnone L. Artigiani S. Chen H. He Z. Ming G. Song H. et al.Plexins are a large family of receptors for transmembrane, secreted and GPI-anchored semaphorins in vertebrates.Cell. 1999; 99: 71-80Abstract Full Text Full Text PDF PubMed Scopus (898) Google Scholar, 3Winberg M.L. Noordermeer J.N. Tamagnone L. Comoglio P.M. Spriggs M.K. Tessier-Lavigne M. Goodman C.S. Plexin A is a neuronal semaphorin receptor that controls axon guidance.Cell. 1998; 95: 903-916Abstract Full Text Full Text PDF PubMed Scopus (367) Google Scholar]. The Rho family GTPases Rho, Rac, and Cdc42 control signal transduction pathways that link plasma membrane receptors to the actin cytoskeleton and thus regulate many actin-driven processes, including cell migration and axon guidance [4Hall A. Rho GTPases and the actin cytoskeleton.Science. 1998; 279: 509-514Crossref PubMed Scopus (5067) Google Scholar, 5Gallo G. Letourneau P.C. Axon guidance GTPases help axons reach their targets.Curr Biol. 1998; 8: 80-82Abstract Full Text Full Text PDF PubMed Google Scholar, 6Ridley A.J. Hall A. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors.Cell. 1992; 70: 389-399Abstract Full Text PDF PubMed Scopus (3717) Google Scholar, 7Ridley A.J. Paterson H.F. Johnston C.L. Diekmann D. Hall A. The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling.Cell. 1992; 70: 401-410Abstract Full Text PDF PubMed Scopus (2984) Google Scholar]. Using yeast two-hybrid screening and in vitro interaction assays, we show that Rac in its active, GTP bound state interacts directly with the cytoplasmic domain of mammalian and Drosophila B plexins. Plexin-B1 clustering in fibroblasts does not cause the formation of lamellipodia, which suggests that Rac is not activated. Instead, it results in the assembly of actin:myosin filaments and cell contraction, which indicates Rho activation. Surprisingly, these cytoskeletal changes are both Rac and Rho dependent. Clustering of a mutant plexin, lacking the Rac binding region, induced similar cytoskeletal changes, and this finding indicates that the physical interaction of plexin-B1 with Rac is not required for Rho activation. Our findings that plexin-B signaling to the cytoskeleton is both Rac and Rho dependent form a starting point for unraveling the mechanism by which semaphorins and plexins control axon guidance and cell migration." @default.
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• W2085751189 date "2001-03-01" @default.
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• W2085751189 title "Plexin-B semaphorin receptors interact directly with active Rac and regulate the actin cytoskeleton by activating Rho" @default.
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• W2085751189 doi "https://doi.org/10.1016/s0960-9822(01)00092-6" @default.
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