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• W2054900513 abstract "The activation mechanisms of Src family kinases (SFKs) involve the dissociation of the intramolecular interaction between the Src homology (SH) 3 and kinase domain. This process is mediated by the intermolecular attack of outer ligands to the SH3 domain. By using a yeast two-hybrid screen, we isolated a relevant ligand involved in the activation mechanisms of SFKs. This molecule was found to be identical to a recently recognized kinetochore protein – designated as centromere protein (CENP)-V – which is required for the progression of mitosis. We show here that human CENP-V plays further roles in cell dynamics; the proline-rich region of human CENP-V associates with the SH3 domains of SFKs and potently activates SFKs, whereas another domain of CENP-V that possesses a highly conserved cysteine array confers the ability to associate with stabilized microtubules (MTs). Human CENP-V distributes to the cell protrusion and to the leading edge of migrating cells in response to external stimuli, and depletion of CENP-V by RNA interference significantly attenuates closure of a scratch wound. These findings indicate that human CENP-V is involved in directional cell motility as well as in the progression of mitosis, as a scaffolding molecule that links MTs and SFKs." @default.
• W2054900513 created "2016-06-24" @default.
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• W2054900513 date "2009-12-01" @default.
• W2054900513 modified "2023-10-01" @default.
• W2054900513 title "Identification of CENP-V as a novel microtubule-associating molecule that activates Src family kinases through SH3 domain interaction" @default.
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• W2054900513 doi "https://doi.org/10.1111/j.1365-2443.2009.01355.x" @default.
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