Regulation of protein activities by phosphoinositide phosphates

被引:60
作者
Niggli, V [1 ]
机构
[1] Univ Bern, Dept Pathol, CH-3010 Bern, Switzerland
关键词
cytoskeleton; phosphatidylinositol 4,5-bisphosphate; phosphatidylinositol 3,4,5-trisphosphate; plasma membrane; actin-membrane linkage;
D O I
10.1146/annurev.cellbio.21.021704.102317
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Phosphoinositide phosphates (PIPs) correspond to phosphorylated derivatives of phosphatidylinositol (PI). Despite their relatively low abundance in the plasma membrane, PIPs play a crucial role as precursors of second messengers and are them selves important sign a ling and targeting molecules. Indeed, modulation of levels of PIPs affects, for example, cortical actin organization, membrane dynamics, and cell migration. The focus of this review is on selected interesting targets of PIPs. Those proteins that bind PIN and are involved in regulation of actin assembly, actin membrane linkage, and actin contractility are discussed, as well as those that are involved in signaling, such as small GTPases, protein kinases, and phosphatases, or in regulation of membrane dynamics.
引用
收藏
页码:57 / 79
页数:23
相关论文
共 111 条
  • [1] Achiriloaie M, 1999, MOL CELL BIOL, V19, P1410
  • [2] Annexins in cell membrane dynamics:: Ca2+-regulated association of lipid microdomains
    Babiychuk, EB
    Draeger, A
    [J]. JOURNAL OF CELL BIOLOGY, 2000, 150 (05) : 1113 - 1123
  • [3] PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    Bai, JH
    Tucker, WC
    Chapman, ER
    [J]. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2004, 11 (01) : 36 - 44
  • [4] Crystal structure of the vinculin tail suggests a pathway for activation
    Bakolitsa, C
    de Pereda, JM
    Bagshaw, CR
    Critchley, DR
    Liddington, RC
    [J]. CELL, 1999, 99 (06) : 603 - 613
  • [5] Structural basis for vinculin activation at sites of cell adhesion
    Bakolitsa, C
    Cohen, DM
    Bankston, LA
    Bobkov, AA
    Cadwell, GW
    Jennings, L
    Critchley, DR
    Craig, SW
    Liddington, RC
    [J]. NATURE, 2004, 430 (6999) : 583 - 586
  • [6] Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution
    Barret, C
    Roy, C
    Montcourrier, P
    Mangeat, P
    Niggli, V
    [J]. JOURNAL OF CELL BIOLOGY, 2000, 151 (05) : 1067 - 1079
  • [7] Phosphatidylinositol 4,5-biphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2
    Benesch, S
    Lommel, S
    Steffen, A
    Stradal, TEB
    Scaplehorn, N
    Way, M
    Wehland, J
    Rottner, K
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (40) : 37771 - 37776
  • [8] Berg JS, 2000, J CELL SCI, V113, P3439
  • [9] Polyphosphoinositides-dependent regulation of the osteoclast actin cytoskeleton and bone resorption
    Biswas, RS
    Baker, DA
    Hruska, KA
    Chellaiah, MA
    [J]. BMC CELL BIOLOGY, 2004, 5 (1)
  • [10] Regulation of WASP/WAVE proteins: making a long story short
    Bompard, G
    Caron, E
    [J]. JOURNAL OF CELL BIOLOGY, 2004, 166 (07) : 957 - 962