High concentrations of phosphatidylinositol-4,5-bisphosphate may promote actin filament growth by three potential mechanisms: Inhibiting capping by neutrophil lysates, severing actin filaments and removing capping protein-β2 from barbed ends

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1358, Issue 3, 1997, Pages 261-278

  Dinubile, Mark J ^a   Huang, Sherry ^a  

^a Department of Surgery   (United States)

Author keywords

Actin; Capping protein 2; Phosphatidylinositol 4,5 bisphosphate (PIP2)

Indexed keywords

F ACTIN; G ACTIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE;

ACTIN FILAMENT; ANIMAL CELL; ARTICLE; CAPPING PHENOMENON; CELL MIGRATION; CONTROLLED STUDY; NEUTROPHIL; NONHUMAN; PRIORITY JOURNAL; RABBIT;

ACTIN DEPOLYMERIZING FACTORS; ACTINS; ANIMALS; BLOOD PROTEINS; CHEMOTAXIS, LEUKOCYTE; CYTOSKELETON; DESTRIN; KINETICS; MICROFILAMENT PROTEINS; MUSCLE, SKELETAL; NEUTROPHILS; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; RABBITS; REGRESSION ANALYSIS; TISSUE EXTRACTS;

EID: 0030833883     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(97)00076-1     Document Type: Article

References (52)

1. Wessells N.K., Spooner B.S., Ash J.F., Bradley M.O., Luduena M.A., Taylor E.L., Wrenn J.T., Yamada K. Microfilaments in cellular and developmental processes. Science. 171:1971;135-143.
2. Axline S.G., Reaven E.P. Inhibition of phagocytosis and plasma membrane mobility of the cultivated macrophage by cytochalasin B. Role of subplasmalemmal microfilaments. J. Cell Biol. 62:1974;647-659.
3. MacLean-Fletcher S., Pollard T.D. Mechanism of action of cytochalasin B on actin. Cell. 20:1980;329-341.
4. White J.R., Naccache P.H., Sha'Afi R.I. Stimulation by chemotactic factors of actin association with cytoskeleton in rabbit neutrophils (role of calcium and cytochalasin). J. Biol. Chem. 258:1983;14041-14047.
5. Cooper J.A. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105:1987;1473-1478.
6. Cassimeris L.U., McNeill H., Zigmond S.H. Chemoattractant-stimulated polymorphonuclear leukocytes contain two populations of actin filaments that differ in their spatial distributions and relative stabilities. J. Cell Biol. 110:1990;1067-1075.
7. Theriot J.A., Mitchison T.J. Actin microfilament dynamics in locomoting cells. Nature. 352:1991;126-131.
8. Fechheimer M., Zigmond S.H. Focusing on unpolymerized actin. J. Cell Biol. 123:1993;1-5.
9. Cano M.L., Lauffenburger D.A., Zigmond S.H. Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution. J. Cell Biol. 115:1991;677-687.
10. Redmond T., Tardif M., Zigmond S.H. Induction of actin polymerization in permeabilized neutrophils. J. Biol. Chem. 269:1994;21657-21663.
11. Stossel T.P. From signal to pseudopod. How cells control cytoplasmic actin assembly. J. Biol. Chem. 264:1989;18261-18264.
12. Hartwig J.H., Bokoch G.M., Carpenter C.L., Janmey P.A., Taylor L.A., Toker A., Stossel T.P. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell. 82:1995;643-653.
13. Janmey P.A., Stossel T.P. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature. 325:1987;362-364.
14. Janmey P.A., Iida K., Yin H.L., Stossel T.P. Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin. J. Biol. Chem. 262:1987;12228-12236.
15. 2. Mol. Biol. Cell. 6:1995;1659-1671.
16. Heiss S.G., Cooper J.A. Regulation of cap Z, an actin capping protein of chicken muscle, by anionic phospholipids. Biochemistry. 30:1991;8753-8758.
17. Schafer D.A., Jennings P.B., Cooper J.A. Dynamics of capping protein interaction with actin filaments. Mol. Biol. Cell. 6(820):1995;141a.
18. Hartwig J.H. Mechanism of actin rearrangements mediating platelet activation. J. Cell Biol. 118:1992;1421-1442.
19. Sullivan S.J., Zigmond S.H. Chemotactic peptide receptor modulation in polymorphonuclear leukocytes. J. Cell Biol. 85:1980;703-711.
20. Klempner M.S., Mikkelsen R.B., Corfman D.H., Andre-Schwartz J. Neutrophils plasma membranes I. High-yield purification of human neutrophil plasma membrane vesicles by nitrogen cavitation and differential centrifugation. J. Cell Biol. 86:1980;21-28.
21. Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:1971;4866-4871.
22. Murray J.M., Weber A., Knox M.K. Myosin subfragment I binding to relaxed actin filaments and the steric model of relaxation. Biochemistry. 20:1981;641-649.
23. Casella J.F., Maack D.J., Lin S. Purification and initial characterization of a protein from skeletal muscle that caps the barbed ends of actin filaments. J. Biol. Chem. 261:1986;10915-10921.
24. Sundler R., Albert A.W., Vagelos P.R. Enzymatic properties of phosphatidylinositol inositolphosphohydrolase from Bacillus cereus. Substrate dilution in detergent-phospholipid micelles and bilayer vesicles. J. Biol. Chem. 253:1978;4175-4179.
25. Maun N.A., Speicher D.W., DiNubile M.J., Southwick F.S. Human cap Z: Purification and properties of a barbed-end actin filament capping protein in human polymorphonuclear leukocytes. Biochem. 35:1996;3518-3524.
26. Casella J.F., Barron-Casella E.A., Torres M.A. Quantitation of cap Z in conventional actin preparations and methods for further purification of actin. Cell Motil. Cyto. 30:1995;164-170.
27. Janmey P.A. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56:1994;169-191.
28. Janmey P.A., Stossel T.P. Gelsolin-polyphosphoinositide interaction: Full expression of gelsolin-inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation, or masking of the inositol head group. J. Biol. Chem. 264:1989;4825-4831.
29. Barkalow K., Witke W., Kwiatkowski D.J., Hartwig J.H. Coordinated regulation of platelet actin filament barbed ends gy gelsolin and capping protein. J. Cell Biol. 134:1996;389-399.
30. Janmey P.A., Lamb J., Allen P.G., Matsudaira P.T. Phosphoinositide-binding peptides derived from the sequence of gelsolin and villin. J. Biol. Chem. 267:1992;11818-11823.
31. Goldschmidt-Clermont P.J., Kim J.W., Machesky L.M., Rhee S.G., Pollard T.D. Regulation of phospholipase C-γ 1 by profilin and tyrosine phosphorylation. Science. 251:1991;1231-1233.
32. Schafer D.A., Jennings P.B., Cooper J.A. Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by phosphoinositides. J. Cell Biol. 135:1996;169-179.
33. Haus U., Trommler P., Fisher P.R., Hartmann H., Lottspeich F., Noegel A.A., Schleicher M. The heat shock cognate protein from Dictyostelium affects actin polymerization through interaction with the actin-binding protein cap32/34. EMBO J. 12:1993;3763-3771.
34. Boyles J., Bainton D.F. Changing patterns of plasma membrane-associated filaments during the initial phases of polymorphonuclear leukocyte adherence. J. Cell Biol. 82:1979;347-368.
35. Boyles J., Bainton D.F. Changes in plasma-membrane-associated filaments during endocytosis and exocytosis in polymorphonuclear leukocytes. Cell. 24:1981;905-914.
36. Hitt A.L., Luna E.J. Membrane interactions with the actin cytoskeleton. Curr. Opin. Cell Biol. 6:1994;120-130.
37. Pestonjamasp K., Amieva M.R., Strassel C.P., Nauseef W.M., Furthmayr H., Luna E.J. Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes. Mol. Biol. Cell. 6:1995;247-259.
38. Pring M., Weber A., Bubb M.R. Profilin-actin complexes directly elongate actin filaments at the barbed end. Biochemistry. 31:1992;1827-1836.
39. 4. Cell. 75:1993;1007-1014.
40. Tardif M., Huang S., Redmond T., Safer D., Pring M., Zigmond S.H. Actin polymerization induced by GTPγS in permeabilized neutrophils is induced and maintained by free barbed ends. J. Biol. Chem. 270:1995;28075-28083.
41. Tilney L.G., Portnoy D.A. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J. Cell Biol. 109:1989;1597-1608.
42. Sanger J.M., Sanger J.W., Southwick F.S. Host cell actin assembly is necessary and likely to provide the propulsive force for intracellular movement of Listeria monocytogenes. Infect. Immun. 60:1992;3609-3619.
43. Kocks C., Gouin E., Tabouret M., Berche P., Ohayon H., Cossart P. Listeria monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell. 68:1992;521-531.
44. Theriot J.A., Rosenblatt J., Portnoy D.A., Goldschmidt-Clermont P.J., Mitchison T.J. Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts. Cell. 76:1994;505-517.
45. Tilney L.G., Connelly P.S., Portnoy D.A. Actin filament nucleation by the bacterial pathogen, Listeria monocytogenes. J. Cell Biol. 111:1990;2979-2988.
46. Tilney L.G., DeRosier D.J., Weber A., Tilney M.S. How Listeria exploits host cell actin to form its own cytoskeleton. II. Nucleation, actin filament polarity, filament assembly, and evidence for a pointed end capper. J. Cell Biol. 118:1992;83-93.
47. DiNubile M.J., Smith E.R., Southwick F.S. Supernatants from Listeria monocytogenes increase the rate of actin polymerization in macrophage extracts. Clin Res. 39:1991;223.
48. Kuhn M., Prevost M.C., Mounier J., Sansonetti P.J. A nonvirulent mutant of Listeria monocytogenes does not move intracellularly but still induces polymerization of actin. Infect. Immun. 58:1990;3477-3486.
49. Sanders M.C., Fung D.C., Theriot J.A. Host cell proteins involved in rapid actin-based motility of intracellular Listeria monocytogenes. Mol. Biol. Cell. 6(1328):1995;229a.
50. Welch M.D., Iwamatsu A., Mitchison T.J. Actin polymerization is induced by arp2/3 protein complex at the surface of Listeria monocytogenes. Nature. 385:1997;265-268.
51. Machesky L.M., Atkinson S.J., Ampe C., Vandekerckhove J., Pollard T.D. Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J. Cell Biol. 127:1994;107-115.
52. Theriot J.A., Mitchison T.J. The three faces of profilin. Cell. 75:1993;835-838.