tailieunhanh - Báo cáo khoa học: Verprolin function in endocytosis and actin organization Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain

Vrp1p (verprolin, End5p) is the yeast ortholog of human Wiskott–Aldrich syndrome protein (WASP)-interacting protein (WIP). Vrp1p localizes to the cortical actin cytoskeleton, is necessary for its polarization to sites of growth and is also essential for endocytosis. At elevated temperature, Vrp1p becomes essential for growth. | ỊFEBS Journal Verprolin function in endocytosis and actin organization Roles of the Las17p yeast WASP -binding domain and a novel C-terminal actin-binding domain Thirumaran Thanabalu1 2 Rajamuthiah Rajmohan2 Lei Meng2 Gang Ren4 5 Parimala R. Vajjhala4 and Alan L. Munn1 3 4 6 1 Institute of Molecular and Cell Biology A STAR BiomedicalScience Institutes Singapore 2 Schoolof BiologicalSciences Nanyang TechnologicalUniversity Singapore 3 Department of Biochemistry Yong Loo Lin Schoolof Medicine The NationalUniversity of Singapore Singapore 4 Institute for Molecular Bioscience and ARC SpecialResearch Centre for Functionaland Applied Genomics The University of Queensland St Lucia Australia 5 UMR7156 CNRS Universite Louis Pasteur Strasbourg France 6 Schoolof BiomedicalSciences The University of Queensland St Lucia Australia Keywords actin patch Arp2 3 Bee1p cell polarity WH2 domain Correspondence A. Munn Institute for Molecular Bioscience The University of Queensland St Lucia Queensland 4072 Australia Fax 61 7 3346 2101 Tel 61 7 3346 2017 E-mail Present address Institute for Molecular Bioscience The University of Queensland St Lucia Australia Received 11 April2007 revised 22 May 2007 accepted 12 June 2007 doi Vrplp verprolin End5p is the yeast ortholog of human Wiskott-Aldrich syndrome protein WASP -interacting protein WIP . Vrp1p localizes to the cortical actin cytoskeleton is necessary for its polarization to sites of growth and is also essential for endocytosis. At elevated temperature Vrp1p becomes essential for growth. A C-terminal Vrp1p fragment C-Vrp1p retains the ability to localize to the cortical actin cytoskeleton and function in actin-cytoskeleton polarization endocytosis and growth. Here we demonstrate that two submodules in C-Vrp1p are required for actin-cytoskeleton polarization a novel C-terminal actin-binding submodule CABS that contains a novel G-actin-binding domain which we call a verprolin homology