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• W3038291132 endingPage "1112" @default.
• W3038291132 startingPage "1101" @default.
• W3038291132 abstract "Plexins receive guidance cues from semaphorin ligands and transmit their signal through the plasma membrane. This family of proteins is unique amongst single-pass transmembrane receptors as their intracellular regions interact directly with several small GTPases, which regulate cytoskeletal dynamics and cell adhesion. Here, we characterize the GTPase Activating Protein (GAP) function of Plexin-B1 and find that a cooperative GAP activity towards the substrate GTPase, Rap1b, is associated with the N-terminal Juxtamembrane region of Plexin-B1. Importantly, we unveil an activation mechanism of Plexin-B1 by identifying a novel functional loop which partially blocks Rap1b entry into the plexin GAP domain. Consistent with the concept of allokairy developed for other systems, Plexin-B activity is increased by an apparent substrate-mediated cooperative effect. Simulations and mutagenesis suggest the repositioned JM conformation is stabilized by the new activation switch loop when the active site is occupied, giving rise to faster enzymatic turnover and cooperative behavior. The biological implications, essentially those of a threshold behavior for cell migration, are discussed." @default.
• W3038291132 created "2020-07-10" @default.
• W3038291132 creator A5030930581 @default.
• W3038291132 creator A5054510775 @default.
• W3038291132 creator A5056319434 @default.
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• W3038291132 date "2020-06-29" @default.
• W3038291132 modified "2023-10-18" @default.
• W3038291132 title "Plexin-Bs enhance their GAP activity with a novel activation switch loop generating a cooperative enzyme" @default.
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• W3038291132 doi "https://doi.org/10.1007/s00018-020-03571-2" @default.
• W3038291132 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7769916" @default.
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• W3038291132 hasPublicationYear "2020" @default.
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