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Functions of Vrp1p in cytokinesis and actin patches are distinct and neither requires a WH2/V domain
Author(s) -
Thanabalu Thirumaran,
Munn Alan L.
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.24.6979
Subject(s) - cytokinesis , biology , microbiology and biotechnology , actin , cleavage furrow , cytoskeleton , myosin , actin remodeling , actin cytoskeleton , wiskott–aldrich syndrome protein , cell division , cell , genetics
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‐Vrp1 1–364 and C‐Vrp1 364–817 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.