The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy Gang Ren,1,4 Parimala Vajjhala,1 Janet S

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The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy Gang Ren,1,4 Parimala Vajjhala,1 Janet S MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, Mar. 2006, p. 37–120 Vol. 70, No. 1 1092-2172/06/$08.00ϩ0 doi:10.1128/MMBR.70.1.37–120.2006 Copyright © 2006, American Society for Microbiology. All Rights Reserved. The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy Gang Ren,1,4 Parimala Vajjhala,1 Janet S. Lee,1 Barbara Winsor,4 and Alan L. Munn1,2,3* 1 2 Institute for Molecular Bioscience, ARC Special Research Centre for Functional and Applied Genomics, and School of Downloaded from Biomedical Sciences,3 University of Queensland, St. Lucia, Queensland 4072, Australia, and UMR7156, Centre National Recherche Scientifique, Universite´Louis Pasteur, Strasbourg 67084, France4 INTRODUCTION .........................................................................................................................................................39 BUDDING YEAST Rvs PROTEINS...........................................................................................................................40 Nutrient Availability and the Control of Cell Proliferation ...............................................................................40 Rvs161p and Rvs167p Proteins and Their Common BAR Domain...................................................................40 BAR Domains of Rvs161p and Rvs167p Assemble into Heterodimers .............................................................40 Loss of Rvs161p or Rvs167p Causes a Similar and Diverse Spectrum of Phenotypes ..................................42 http://mmbr.asm.org/ Reduced viability upon starvation (Rvs؊).........................................................................................................42 Growth sensitivity to salt (especially Na؉).......................................................................................................42 Growth sensitivity to cytotoxic compounds .......................................................................................................42 Growth sensitivity to elevated temperature.......................................................................................................43 Growth on nonfermentable carbon sources ......................................................................................................43 Meiosis and sporulation ......................................................................................................................................43 Heterogeneous cell size and morphology upon starvation or exposure to Na؉ ..........................................43 Loss of actin cytoskeleton polarization to sites of polarized growth.............................................................43 Delocalized cell wall chitin deposition....................................................................................................44 Loss of bipolar bud site selection.......................................................................................................................44 on October 26, 2015 by University of Queensland Library Defective fluid-phase and receptor-mediated endocytosis...............................................................................44 Inefficient cell-cell fusion during mating...........................................................................................................44 Rvs161p and Rvs167p Structure-Function Relationships...................................................................................45 Rvs Proteins Localize to the Cortical Actin Cytoskeleton ..................................................................................45 Subcellular localization of Rvs161p and Rvs167p............................................................................................45 Interactions between Rvs167p and actin patch proteins.................................................................................47 Roles of Rvs161p and Rvs167p in Endocytosis ....................................................................................................49 Rvs161p and Rvs167p in receptor-mediated internalization of ␣-factor......................................................49 Role for Rvs161p and Rvs167p in postinternalization trafficking through endosomes?............................57 Roles of Rvs161p and Rvs167p in the Secretory Pathway ..................................................................................58 Rvs161p and Rvs167p are not essential for all secretory membrane traffic................................................58 Rvs proteins may be required for polarized secretion during cell division .................................................58 Rvs proteins and post-Golgi apparatus traffic .................................................................................................58 Rvs proteins and ER-to-Golgi apparatus traffic...............................................................................................59 Rvs proteins and mating......................................................................................................................................59 rvs Mutations Interact with Actin and Myosin Mutations .................................................................................63 Rvs؊ phenotypes are associated with mutations affecting other actin cytoskeleton proteins ...................63 Genetic interactions between Rvs proteins and actin......................................................................................67 Genetic interactions between Rvs proteins and yeast myosins ......................................................................67 Rvs Proteins and Membranes.................................................................................................................................68 Association of cortical actin cytoskeleton with membranes............................................................................68 Fractionation of Rvs proteins with membranes ...............................................................................................68 Rvs proteins and lipid rafts ................................................................................................................................68 Suppression of Rvs؊ phenotypes by mutations affecting glycosphingolipid biosynthesis..........................69 Regulation of Rvs167p by Phosphorylation ..........................................................................................................72 Regulation of Rvs167p by Ubiquitination .............................................................................................................73 Genomic and Proteomic Approaches and the Diverse Network of Rvs Interactions......................................74 Large-scale two-hybrid screens for Rvs161p- and Rvs167p-interacting proteins ........................................74 Identification of Rvs167p SH3 domain-interacting proteins by phage display............................................74 Identification of Rvs161p- and Rvs167p-interacting proteins by high-throughput proteomics.................74 Mapping the genetic interactions of Rvs161p and Rvs167p by synthetic genetic array.............................74 Rvs161p and Rvs167p physical and genetic interactions suggest multiple functions in vivo....................74 * Corresponding author. Mailing address: Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia. Phone: 61-7-3346 2017. Fax: 61-7-3346 2101. E-mail: a.munn @imb.uq.edu.au. 37 38 REN ET AL. MICROBIOL.MOL.BIOL.REV. FISSION YEAST BAR DOMAIN PROTEINS Hob1p AND Hob3p......................................................................75 Hob3p, Fission Yeast Ortholog of Rvs161p ..........................................................................................................75 Hob3p has a domain structure similar to that of Rvs161p............................................................................75 Hob3p functions in polarization of the cortical actin cytoskeleton but not endocytosis............................75 Functional conservation between Hob3p, Rvs161p, and human Bin3.....................................................................75 Hob1p, Fission Yeast Ortholog of Rvs167p ..........................................................................................................75 Hob1p has a domain structure similar to that of Rvs167p............................................................................75 Hob1p is not required for polarization of the cortical actin cytoskeleton or endocytosis .........................75 Hob1p interacts with actin assembly proteins and protein kinases that regulate cell polarity................76 Downloaded from Hob1p functions in regulating cell cycle progression in response to nutrient availability........................76 Functional Conservation of Hob1p and Bin1 and Divergence of Rvs167p ......................................................76 Hob1p functions in regulation of cell cycle progression in response to DNA damage...............................76 Hob1p functions in a cell stress signal transduction pathway upstream of Hob3p ...................................77 VERTEBRATE BAR DOMAIN PROTEIN AMPHIPHYSIN 1 ..............................................................................77 Endocytic Recycling of Synaptic Vesicles ..............................................................................................................77 Role of dynamin 1 in synaptic vesicle recycling ...............................................................................................77
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