The verprolin family of proteins: regulators of cell morphogenesis and endocytosis.
The verprolin family of proteins, WIP, CR16 and WIRE/WICH, has emerged as critical regulators of cytoskeletal organisation in vertebrate cells. The founding father of the family, verprolin, was originally identified in budding yeast and later shown to be needed for actin polymerisation during polarised growth and during endocytosis. The vertebrate verprolins regulate actin dynamics either by binding directly to actin, by binding the WASP family of proteins or by binding to other actin regulating proteins. Interestingly, also the vertebrate verprolins have been implicated in endocytosis, demonstrating that most of the functional modules in this fascinating group of proteins have been conserved from yeast to man.
Aspenström
Pontus
P
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala University, Sweden. pontus.aspenstroms@LICR.uu.se
D000199:Actins / Q000502:physiology; D000595:Amino Acid Sequence; D000818:Animals; D004705:Endocytosis / Q000502:physiology*; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry / Q000502:physiology*; D008969:Molecular Sequence Data; D009024:Morphogenesis / Q000502:physiology*; D017386:Sequence Homology, Amino Acid
D000199:Actins; D008840:Microfilament Proteins