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|Title:||Functions of Vrp1p in cytokinesis and actin patches are distinct and neither requires a WH2/V domain||Authors:||Thanabalu, T.
|Issue Date:||17-Dec-2002||Citation:||Thanabalu, T., Munn, A.L. (2002-12-17). Functions of Vrp1p in cytokinesis and actin patches are distinct and neither requires a WH2/V domain. EMBO Journal 20 (24) : 6979-6989. ScholarBank@NUS Repository. https://doi.org/10.1093/emboj/20.24.6979||Abstract:||Vrp1 (verprolin, End5) is a Saccharomyces cerevisiae actin-associated protein and is related to mammalian Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP). Vrp1-deficient (vrp1Δ) cells are inviable at high temperature, have partially depolarized cortical actin patches and have defects in both actomyosin ring-dependent and Hof1 (Cyk2)-dependent pathways of cytokinesis. We demonstrate here that N-Vrp11-364 and C-Vrp1364-817 are each sufficient to restore viability, actomyosin ring constriction and Hof1 localization at 37°C to vrp1Δ. C-Vrp1, like Vrp1, partially co-localizes with cortical actin patches and restores actin patch polarization to vrp1Δ. Cortical localization of C-Vrp1, but not Vrp1, requires Las17. N-Vrp1 exhibits diffuse cytoplasmic localization and functions in cytokinesis without efficiently restoring polarization of cortical actin patches. N-Vrp1 function is not abolished by mutations affecting the WASP homology 2 (WH2) [verprolin homology (V)] actin-binding domain. N-Vrp1 may function through the type I myosins and actin, while C-Vrp1 may function through both Las17 (Bee1) and type I myosins. The functions of Vrp1 in viability at 37°C and cytokinesis do not require efficient localization to, and function in, the cortical actin cytoskeleton.||Source Title:||EMBO Journal||URI:||http://scholarbank.nus.edu.sg/handle/10635/111894||ISSN:||02614189||DOI:||10.1093/emboj/20.24.6979|
|Appears in Collections:||Staff Publications|
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