title: Verprolin: a cool set of actin-binding sites and some very HOT prolines.
abstract: Spatiotemporal organisation of eukaryotic cells is established and maintained by the cytoskeleton, a highly dynamic and complex network of structural and signalling proteins. Many components of the cytoskeleton are functionally and structurally conserved between humans and yeast. Among these are verprolin (Vrp1p) in yeast and its human ortholog Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP). Much of our understanding of the function of these proteins has come from genetic analysis in yeast. Verprolin-deficient yeast cells exhibit defects in cytokinesis, endocytosis, and actin cytoskeleton polarisation. Verprolin binds actin, the yeast ortholog of human WASP (Las17p or Bee1p), and the yeast ortholog of human PSTPIP1 (Hof1p or Cyk2p). We propose that verprolin acts as a chaperone that by transient bimolecular interactions maintains the proper function of its partners. Verprolin-related proteins and partners are implicated in cancer, immunodeficiency, and neurodegeneration. Therefore, elucidating how verprolin functions will have major impacts in cell biology and medicine.
authors.affiliation: School of Medical Science and Molecular Basis of Disease Programme, Griffith University, Southport, Queensland, Australia. a.munn@griffith.edu.au
authors.forename: Alan L
authors.initials: AL
authors.lastname: Munn
authors.forename: Thirumaran
authors.initials: T
authors.lastname: Thanabalu
mesh_terms: D000199:Actins / Q000378:metabolism*; D000205:Actomyosin / Q000502:physiology; D001665:Binding Sites; D048749:Cytokinesis / Q000502:physiology; D003598:Cytoskeletal Proteins / Q000502:physiology; D004705:Endocytosis / Q000235:genetics; D006801:Humans; D007153:Immunologic Deficiency Syndromes / Q000503:physiopathology; D047908:Intracellular Signaling Peptides and Proteins / Q000502:physiology; D008840:Microfilament Proteins / Q000502:physiology*; D008869:Microtubule-Associated Proteins / Q000502:physiology; D009369:Neoplasms / Q000503:physiopathology; D019636:Neurodegenerative Diseases / Q000503:physiopathology; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology*; D013329:Structure-Activity Relationship
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; C116847:HOF1 protein, S cerevisiae; D047908:Intracellular Signaling Peptides and Proteins; D008840:Microfilament Proteins; D008869:Microtubule-Associated Proteins; D029701:Saccharomyces cerevisiae Proteins; C090350:VRP1 protein, S cerevisiae; C109903:WIPF1 protein, human; D000205:Actomyosin