title: PI(4,5)P(2) regulation of surface membrane traffic.
abstract: Phosphatidylinositol 4,5-biphosphate (PI[4,5]P(2)) has emerged as an important signaling molecule in the membrane for regulating vesicle exo- and endocytosis and the accompanying actin cytoskeletal rearrangements. Localization studies with GFP-tagged binding domains and antibodies provide new views of the non-uniform, dynamic distribution of PI(4,5)P(2) in membranes and its organization in raft-like domains. The targeting of phosphoinositide kinases by GTPases can coordinate the reactions of membrane fusion and fission with cytoskeletal assembly, providing a basis for membrane movement.
authors.affiliation: Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, 53706, Wisconsin, USA. tfmartin@facstaff.wisc.edu
authors.forename: T F
authors.initials: TF
authors.lastname: Martin
mesh_terms: D000818:Animals; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism; D004705:Endocytosis; D006056:Golgi Apparatus / Q000502:physiology; D021962:Membrane Microdomains / Q000737:chemistry; D008954:Models, Biological; D020559:Monomeric GTP-Binding Proteins / Q000502:physiology; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000032:analysis / Q000502:physiology*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000378:metabolism; D022161:Transport Vesicles / Q000378:metabolism
chemical_list: D019269:Phosphatidylinositol 4,5-Diphosphate; D017853:Phosphotransferases (Alcohol Group Acceptor); D020559:Monomeric GTP-Binding Proteins