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  • Verprolin cytokinesis function mediated by the Hof One trap domain
    Ren, Gang ...
    In budding yeast, partitioning of the cytoplasm during cytokinesis can proceedvia a pathway dependent on the contractile actomyosin ring, as in othereukaryotes, or alternatively via a septum ... deposition pathway dependent onan SH3 domain protein, Hof1žCyk2 (the yeast PSTPIP1 ortholog). In dividing yeast cells, Hof1 forms a ring at the bud neck distinct from the actomyosin ring, and this zone is active in septum deposition. We previously showed the yeast WiskottAldrich syndrome protein (WASP)-interacting protein (WIP) ortholog, verprolinžVrp1žEnd5, interacts with Hof1 and facilitates Hof1 recruitment to the bud neck. A Vrp1 fragment unable to interact with yeast WASP (Las17žBee1), localize to the actin cytoskeleton or function in polarization of the cortical actin cytoskeleton nevertheless retains function in Hof1 recruitment and cytokinesis. Here, we show the ability of this Vrp1 fragment to bind the Hof1 SH3 domain via its Hof one trap (HOT) domain is critical for cytokinesis. The Vrp1 HOT domain consists of three tandem proline-rich motifs flanked by serines. Unexpectedly, the Hof1 SH3 domain itself is not required for cytokinesis and indeed appears to negatively regulate cytokinesis. The Vrp1 HOT domain promotes cytokinesis by binding to the Hof1 SH3 domain and counteracting its inhibitory effect.
    Vrsta gradiva - članek, sestavni del
    Leto - 2005
    Jezik - angleški
    COBISS.SI-ID - 3310618