메뉴 건너뛰기




Volumn 65, Issue , 2003, Pages 761-789

Phosphoinositide Regulation of the Actin Cytoskeleton

Author keywords

Actin nucleation; Actin membrane linkage; Phosphatidylinositol 4,5 bisphosphate

Indexed keywords

ACTIN; ALPHA ACTININ; ARF PROTEIN; BINDING PROTEIN; EZRIN; FILAMIN; GUANOSINE TRIPHOSPHATASE; LIPID; MOESIN; PHOSPHATIDYLINOSITIDE; RADIXIN; REGULATOR PROTEIN; TALIN; VINCULIN; PHOSPHATIDYLINOSITOL;

EID: 0038311944     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.65.092101.142517     Document Type: Review
Times cited : (588)

References (170)
  • 1
    • 0022430243 scopus 로고
    • Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide
    • Anderson RA, Marchesi VT. 1985. Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide. Nature 318:295-98
    • (1985) Nature , vol.318 , pp. 295-298
    • Anderson, R.A.1    Marchesi, V.T.2
  • 2
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5 bisphosphate and profilactin
    • Lassing I, Lindberg U. 1985. Specific interaction between phosphatidylinositol 4,5 bisphosphate and profilactin. Nature 314:472-74
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 3
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey PA, Stossel TP. 1987. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 325:362-64
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 4
    • 0035424240 scopus 로고    scopus 로고
    • PI(4,5)P(2) Regulation of surface membrane traffic
    • Martin TF. 2001. PI(4,5)P(2) Regulation of surface membrane traffic. Curr. Opin. Cell Biol. 13:493-99
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 5
    • 0035980759 scopus 로고    scopus 로고
    • Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane
    • Takenawa T, Itoh T. 2001. Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane. Biochim. Biophys. Acta 1533:190-206
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 190-206
    • Takenawa, T.1    Itoh, T.2
  • 7
    • 0035074215 scopus 로고    scopus 로고
    • Phosphoinositides in membrane traffic at the synapse
    • Cremona O, De Camilli P. 2001. Phosphoinositides in membrane traffic at the synapse. J. Cell Sci. 114:1041-52
    • (2001) J. Cell Sci. , vol.114 , pp. 1041-1052
    • Cremona, O.1    De Camilli, P.2
  • 8
    • 0033677862 scopus 로고    scopus 로고
    • The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane
    • Sechi AS, Wehland J. 2000. The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane. J. Cell Sci. 113(Pt 21):3685-95
    • (2000) J. Cell Sci. , vol.113 , Issue.21 PART , pp. 3685-3695
    • Sechi, A.S.1    Wehland, J.2
  • 9
    • 0035910461 scopus 로고    scopus 로고
    • Regulation of apoptosis by phosphatidylinositol 4,5 bisphosphate inhibition of caspases, and caspase inactivation of phosphatidylinositol phosphate 5-kinases
    • Mejillano M, Yamamoto M, Rozelle AL, Sun HQ, Wang X, Yin HL. 2001. Regulation of apoptosis by phosphatidylinositol 4,5 bisphosphate inhibition of caspases, and caspase inactivation of phosphatidylinositol phosphate 5-kinases. J. Biol. Chem. 276:1865-72
    • (2001) J. Biol. Chem. , vol.276 , pp. 1865-1872
    • Mejillano, M.1    Yamamoto, M.2    Rozelle, A.L.3    Sun, H.Q.4    Wang, X.5    Yin, H.L.6
  • 11
    • 0035975965 scopus 로고    scopus 로고
    • Modular phosphoinositide-binding domains - Their role in signalling and membrane trafficking
    • Cullen PJ, Cozier GE, Banting G, Mellor H. 2001. Modular phosphoinositide-binding domains - their role in signalling and membrane trafficking. Curr. Biol. 11:R882-93
    • (2001) Curr. Biol. , vol.11
    • Cullen, P.J.1    Cozier, G.E.2    Banting, G.3    Mellor, H.4
  • 12
    • 0029978885 scopus 로고    scopus 로고
    • Identification of the binding site for acidic phospholipids on the PH domain of dynamin: Implications for stimulation of GTPase activity
    • Zheng J, Cahill SM, Lemmon MA, Fushman D, Schlessinger J, Cowburn D. 1996. Identification of the binding site for acidic phospholipids on the PH domain of dynamin: implications for stimulation of GTPase activity. J. Mol. Biol. 22:14-21
    • (1996) J. Mol. Biol. , vol.22 , pp. 14-21
    • Zheng, J.1    Cahill, S.M.2    Lemmon, M.A.3    Fushman, D.4    Schlessinger, J.5    Cowburn, D.6
  • 14
    • 0035979372 scopus 로고    scopus 로고
    • Phox homology domains specifically bind phosphatidylinositol phosphates
    • Song X, Xu W, Zhang A, Huang G, Liang X, et al. 2001. Phox homology domains specifically bind phosphatidylinositol phosphates. Biochemistry 40:8940-44
    • (2001) Biochemistry , vol.40 , pp. 8940-8944
    • Song, X.1    Xu, W.2    Zhang, A.3    Huang, G.4    Liang, X.5
  • 15
    • 0035134328 scopus 로고    scopus 로고
    • Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis
    • Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. 2001. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science 291:1047-51
    • (2001) Science , vol.291 , pp. 1047-1051
    • Itoh, T.1    Koshiba, S.2    Kigawa, T.3    Kikuchi, A.4    Yokoyama, S.5    Takenawa, T.6
  • 17
    • 0035793903 scopus 로고    scopus 로고
    • Structural mechanism of endosome docking by the FYVE domain
    • Kutateladze T, Overduin M. 2001. Structural mechanism of endosome docking by the FYVE domain. Science 291:1793-96
    • (2001) Science , vol.291 , pp. 1793-1796
    • Kutateladze, T.1    Overduin, M.2
  • 18
    • 17944367436 scopus 로고    scopus 로고
    • The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate
    • Bravo J, Karathanassis D, Pacold CM, Pacold ME, Ellson CD, et al. 2001. The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol. Cell 8:829-39
    • (2001) Mol. Cell , vol.8 , pp. 829-839
    • Bravo, J.1    Karathanassis, D.2    Pacold, C.M.3    Pacold, M.E.4    Ellson, C.D.5
  • 20
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • Berg JS, Cheney RE. 2002. Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat. Cell Biol. 4:246-50
    • (2002) Nat. Cell Biol. , vol.4 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 21
    • 0032791313 scopus 로고    scopus 로고
    • The pleckstrin homology domain of the Wiskott-Aldrich syndrome protein is involved in the organization of actin cytoskeleton
    • Imai K, Nonoyama S, Miki H, Morio T, Fukami K, et al. 1999. The pleckstrin homology domain of the Wiskott-Aldrich syndrome protein is involved in the organization of actin cytoskeleton. Clin. Immunol. 92:128-37
    • (1999) Clin. Immunol. , vol.92 , pp. 128-137
    • Imai, K.1    Nonoyama, S.2    Miki, H.3    Morio, T.4    Fukami, K.5
  • 22
    • 0035854732 scopus 로고    scopus 로고
    • Nek and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    • Rohatgi R, Nollau P, Ho HY, Kirschner MW, Mayer BJ. 2001. Nek and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway. J. Biol. Chem. 276:26,448-52
    • (2001) J. Biol. Chem. , vol.276 , pp. 26448-26452
    • Rohatgi, R.1    Nollau, P.2    Ho, H.Y.3    Kirschner, M.W.4    Mayer, B.J.5
  • 23
    • 0037086053 scopus 로고    scopus 로고
    • Conserved interactions with cytoskeletal but not signaling elements are an essential aspect of Drosophila WASP function
    • Tal T, Vaizel-Ohayon D, Schejter ED. 2002. Conserved interactions with cytoskeletal but not signaling elements are an essential aspect of Drosophila WASP function. Dev. Biol. 243:260-71
    • (2002) Dev. Biol. , vol.243 , pp. 260-271
    • Tal, T.1    Vaizel-Ohayon, D.2    Schejter, E.D.3
  • 24
    • 0034683671 scopus 로고    scopus 로고
    • Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASP) stimulates actin nucleation by Arp2/3 complex
    • Higgs HN, Pollard TD. 2000. Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASP) stimulates actin nucleation by Arp2/3 complex. J. Cell Biol. 150:1311-20
    • (2000) J. Cell Biol. , vol.150 , pp. 1311-1320
    • Higgs, H.N.1    Pollard, T.D.2
  • 25
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey PA. 1994. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56:169-91
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Janmey, P.A.1
  • 26
    • 0035478249 scopus 로고    scopus 로고
    • Structural properties of lipid-binding sites in cytoskeletal proteins
    • Niggli V. 2001. Structural properties of lipid-binding sites in cytoskeletal proteins. Trends Biochem. Sci. 26:604-11
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 604-611
    • Niggli, V.1
  • 27
    • 0035969971 scopus 로고    scopus 로고
    • Full-contact domain labeling: Identification of a novel phosphoinositide binding site on gelsolin that requires the complete protein
    • Feng L, Mejillano M, Yin HL, Chen J, Prestwich GD. 2001. Full-contact domain labeling: identification of a novel phosphoinositide binding site on gelsolin that requires the complete protein. Biochemistry 40:904-13
    • (2001) Biochemistry , vol.40 , pp. 904-913
    • Feng, L.1    Mejillano, M.2    Yin, H.L.3    Chen, J.4    Prestwich, G.D.5
  • 29
    • 0042354345 scopus 로고    scopus 로고
    • Differential recognition of phosphoinositides by actin regulating proteins and its physiological implications
    • ed. KS Bruzik, Washington, DC: Am. Chem. Soc.
    • Lu P-J, Wang D-S, Lin K-M, Yin HL, Chen C-S. 1999. Differential recognition of phosphoinositides by actin regulating proteins and its physiological implications. In Phosphoinositides. Chemistry, Biochemistry, and Biomedical Applications, ed. KS Bruzik, pp. 38-54. Washington, DC: Am. Chem. Soc.
    • (1999) Phosphoinositides. Chemistry, Biochemistry, and Biomedical Applications , pp. 38-54
    • Lu, P.-J.1    Wang, D.-S.2    Lin, K.-M.3    Yin, H.L.4    Chen, C.-S.5
  • 30
    • 0039291162 scopus 로고    scopus 로고
    • Fluorescent phosphoinositide derivatives reveal specific binding of gelsolin and other actin regulatory proteins to mixed lipid bilayers
    • Tuominen EKJ, Holopainen JM, Chen J, Prestwich GD, Bachiller PR, et al. 1999. Fluorescent phosphoinositide derivatives reveal specific binding of gelsolin and other actin regulatory proteins to mixed lipid bilayers. Eur. J. Biochem. 262:1-9
    • (1999) Eur. J. Biochem. , vol.262 , pp. 1-9
    • Tuominen, E.K.J.1    Holopainen, J.M.2    Chen, J.3    Prestwich, G.D.4    Bachiller, P.R.5
  • 31
    • 0036237488 scopus 로고    scopus 로고
    • Phosphoinositide kinases as enzymes that produce versatile signaling lipids, phosphoinositides
    • Kanaho Y, Suzuki T. 2002. Phosphoinositide kinases as enzymes that produce versatile signaling lipids, phosphoinositides. J. Biochem. 131:503-9
    • (2002) J. Biochem. , vol.131 , pp. 503-509
    • Kanaho, Y.1    Suzuki, T.2
  • 32
    • 0033618375 scopus 로고    scopus 로고
    • PIKfyve, a mammalian ortholog of yeast Fab1p lipid kinase, synthesizes 5-phosphoinositides. Effect of insulin
    • Sbrissa D, Ikonomov OC, Shisheva A. 1999. PIKfyve, a mammalian ortholog of yeast Fab1p lipid kinase, synthesizes 5-phosphoinositides. Effect of insulin. J. Biol. Chem. 274:21589-97
    • (1999) J. Biol. Chem. , vol.274 , pp. 21589-21597
    • Sbrissa, D.1    Ikonomov, O.C.2    Shisheva, A.3
  • 33
    • 0033969444 scopus 로고    scopus 로고
    • The activation loop of phosphatidylinositol phosphate kinases determines signaling specificity
    • Kunz J, Wilson MP, Kisseleva M, Hurley JH, Majerus PW, Anderson RA. 2000. The activation loop of phosphatidylinositol phosphate kinases determines signaling specificity. Mol. Cell 5:1-11
    • (2000) Mol. Cell , vol.5 , pp. 1-11
    • Kunz, J.1    Wilson, M.P.2    Kisseleva, M.3    Hurley, J.H.4    Majerus, P.W.5    Anderson, R.A.6
  • 34
    • 0035861733 scopus 로고    scopus 로고
    • Phosphatidylinositol-4-phosphate 5-kinase-1beta is essential for epidermal growth factor receptor-mediated endocytosis
    • Barbieri MA, Heath CM, Peters EM, Wells A, Davis JN, Stahl PD. 2001. Phosphatidylinositol-4-phosphate 5-kinase-1beta is essential for epidermal growth factor receptor-mediated endocytosis. J. Biol. Chem. 276:47212-16
    • (2001) J. Biol. Chem. , vol.276 , pp. 47212-47216
    • Barbieri, M.A.1    Heath, C.M.2    Peters, E.M.3    Wells, A.4    Davis, J.N.5    Stahl, P.D.6
  • 35
    • 0034740730 scopus 로고    scopus 로고
    • PIP kinase Igamma is the major PI(4,5)P(2) synthesizing enzyme at the synapse
    • Wenk MR, Pellegrini L, Klenchin VA, Di Paolo G, Chang S, et al. 2001. PIP kinase Igamma is the major PI(4,5)P(2) synthesizing enzyme at the synapse. Neuron 32:79-88
    • (2001) Neuron , vol.32 , pp. 79-88
    • Wenk, M.R.1    Pellegrini, L.2    Klenchin, V.A.3    Di Paolo, G.4    Chang, S.5
  • 36
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • Ichetovkin I, Grant W, Condeelis J. 2002. Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr. Biol. 12:79-84
    • (2002) Curr. Biol. , vol.12 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 37
    • 0029926545 scopus 로고    scopus 로고
    • Localization and turnover of phosphatidylinositol 4,5 bisphosphate in caveolin-enriched membrane domains
    • Pike LJ, Casey L. 1996. Localization and turnover of phosphatidylinositol 4,5 bisphosphate in caveolin-enriched membrane domains. J. Biol. Chem. 271:24653-56
    • (1996) J. Biol. Chem. , vol.271 , pp. 24653-24656
    • Pike, L.J.1    Casey, L.2
  • 38
    • 0034234718 scopus 로고    scopus 로고
    • How accurately can we image inositol lipids in living cells?
    • Balla T, Bondeva T, Varnai P. 2000. How accurately can we image inositol lipids in living cells? Trends Pharmacol. Sci. 21:238-41
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 238-241
    • Balla, T.1    Bondeva, T.2    Varnai, P.3
  • 39
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler S, Currie RA, Campbell DG, Deak M, Kular G, et al. 2000. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem. J. 351:19-31
    • (2000) Biochem. J. , vol.351 , pp. 19-31
    • Dowler, S.1    Currie, R.A.2    Campbell, D.G.3    Deak, M.4    Kular, G.5
  • 40
    • 0035954430 scopus 로고    scopus 로고
    • Restricted accumulation of phosphatidylinositol 3-kinase products in a plasmalemmal subdomain during Fc gamma receptor-mediated phagocytosis
    • Marshall JG, Booth JW, Stambolic V, Mak T, Balla T, et al. 2001. Restricted accumulation of phosphatidylinositol 3-kinase products in a plasmalemmal subdomain during Fc gamma receptor-mediated phagocytosis. J. Cell Biol. 153:1369-80
    • (2001) J. Cell Biol. , vol.153 , pp. 1369-1380
    • Marshall, J.G.1    Booth, J.W.2    Stambolic, V.3    Mak, T.4    Balla, T.5
  • 41
  • 42
    • 0037133606 scopus 로고    scopus 로고
    • Neutrophils lacking phosphoinositide 3-kinase gamma show loss of directionality during N-formyl-Met-Leu-Phe-induced chemotaxis
    • Hannigan M, Zhan L, Li Z, Ai Y, Wu D, Huang CK. 2002. Neutrophils lacking phosphoinositide 3-kinase gamma show loss of directionality during N-formyl-Met-Leu-Phe-induced chemotaxis. Proc. Natl. Acad. Sci. USA 99:3603-8
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3603-3608
    • Hannigan, M.1    Zhan, L.2    Li, Z.3    Ai, Y.4    Wu, D.5    Huang, C.K.6
  • 44
    • 0034625410 scopus 로고    scopus 로고
    • A pleckstrin homology domain specific for phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis
    • Holz RW, Hlubek MD, Sorensen SD, Fisher SK, Balla T, et al. 2000. A pleckstrin homology domain specific for phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis. J. Biol. Chem. 275:17878-85
    • (2000) J. Biol. Chem. , vol.275 , pp. 17878-17885
    • Holz, R.W.1    Hlubek, M.D.2    Sorensen, S.D.3    Fisher, S.K.4    Balla, T.5
  • 45
    • 0033601075 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation
    • Honda A, Nogami M, Yokozeki T, Yamazaki M, Nakamura H, et al. 1999. Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation. Cell 99:521-32
    • (1999) Cell , vol.99 , pp. 521-532
    • Honda, A.1    Nogami, M.2    Yokozeki, T.3    Yamazaki, M.4    Nakamura, H.5
  • 46
    • 0035939659 scopus 로고    scopus 로고
    • Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity
    • Micheva KD, Holz RW, Smith SJ. 2001. Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity. J. Cell Biol. 154:355-68
    • (2001) J. Cell Biol. , vol.154 , pp. 355-368
    • Micheva, K.D.1    Holz, R.W.2    Smith, S.J.3
  • 47
    • 0036231070 scopus 로고    scopus 로고
    • Distribution of gelsolin and phosphoinositol 4,5-bisphosphate in lamellipodia during EGF-induced motility
    • Chou J, Stolz DB, Burke NA, Watkins SC, Wells A. 2002. Distribution of gelsolin and phosphoinositol 4,5-bisphosphate in lamellipodia during EGF-induced motility. Int. J. Biochem. Cell Biol. 34:776-90
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 776-790
    • Chou, J.1    Stolz, D.B.2    Burke, N.A.3    Watkins, S.C.4    Wells, A.5
  • 48
    • 0034739859 scopus 로고    scopus 로고
    • Localized biphasic changes in phosphatidylinositol-4,5-bisphosphate at sites of phagocytosis
    • Botelho RJ, Teruel M, Dierckman R, Anderson R, Wells A, et al. 2000. Localized biphasic changes in phosphatidylinositol-4,5-bisphosphate at sites of phagocytosis. J. Cell Biol. 151:1353-68
    • (2000) J. Cell Biol. , vol.151 , pp. 1353-1368
    • Botelho, R.J.1    Teruel, M.2    Dierckman, R.3    Anderson, R.4    Wells, A.5
  • 49
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher D, Stauffer T, Chen W, Shen K, Guo S, et al. 2000. Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell 100: 221-28
    • (2000) Cell , vol.100 , pp. 221-228
    • Raucher, D.1    Stauffer, T.2    Chen, W.3    Shen, K.4    Guo, S.5
  • 50
    • 0036566427 scopus 로고    scopus 로고
    • Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1
    • Watt SA, Kular G, Fleming IN, Downes CP, Lucocq JM. 2002. Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1. Biochem. J. 363:657-66
    • (2002) Biochem. J. , vol.363 , pp. 657-666
    • Watt, S.A.1    Kular, G.2    Fleming, I.N.3    Downes, C.P.4    Lucocq, J.M.5
  • 51
    • 0034607688 scopus 로고    scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the Golgi compartment
    • Jones DH, Morris JB, Morgan CP, Kondo H, Irvine RF, Cockcroft S. 2000. Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the Golgi compartment. J. Biol. Chem. 275:13,962-66
    • (2000) J. Biol. Chem. , vol.275 , pp. 13962-13966
    • Jones, D.H.1    Morris, J.B.2    Morgan, C.P.3    Kondo, H.4    Irvine, R.F.5    Cockcroft, S.6
  • 53
    • 0033580933 scopus 로고    scopus 로고
    • Coupled inositide phosphorylation and phospholipase D activation initiates clathrin-coat assembly on lysosomes
    • Arneson LS, Kunz J, Anderson RA, Traub LM. 1999. Coupled inositide phosphorylation and phospholipase D activation initiates clathrin-coat assembly on lysosomes. J. Biol. Chem. 274:17794-7805
    • (1999) J. Biol. Chem. , vol.274 , pp. 17794-17805
    • Arneson, L.S.1    Kunz, J.2    Anderson, R.A.3    Traub, L.M.4
  • 54
    • 0032736675 scopus 로고    scopus 로고
    • Essential role of phosphoinositide metabolism in synaptic vesicle recycling
    • Cremona O, Di Paolo G, Wenk MR, Luthi A, Kim WT, et al. 1999. Essential role of phosphoinositide metabolism in synaptic vesicle recycling. Cell 99:179-88
    • (1999) Cell , vol.99 , pp. 179-188
    • Cremona, O.1    Di Paolo, G.2    Wenk, M.R.3    Luthi, A.4    Kim, W.T.5
  • 55
    • 0036181710 scopus 로고    scopus 로고
    • The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)-bisphosphate
    • Stefan CJ, Audhya A, Emr SD. 2002. The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)-bisphosphate. Mol. Biol. Cell 13:542-57
    • (2002) Mol. Biol. Cell , vol.13 , pp. 542-557
    • Stefan, C.J.1    Audhya, A.2    Emr, S.D.3
  • 56
    • 0031885535 scopus 로고    scopus 로고
    • Green fluorescent protein as a non-invasive intracellular pH indicator
    • Kneen M, Farinas J, Li Y, Verkman AS. 1998. Green fluorescent protein as a non-invasive intracellular pH indicator. Biophys. J. 74:1591-99
    • (1998) Biophys. J. , vol.74 , pp. 1591-1599
    • Kneen, M.1    Farinas, J.2    Li, Y.3    Verkman, A.S.4
  • 59
    • 0037178885 scopus 로고    scopus 로고
    • Inositol lipid binding and membrane localization of isolated pleckstrin homology domains. Studies on the PH-domains of PLCdelta 1 and p130
    • Varnai P, Lin X, Lee SB, Tuymetova G, Bondeva T, et al. 2002. Inositol lipid binding and membrane localization of isolated pleckstrin homology domains. Studies on the PH-domains of PLCdelta 1 and p130. J. Biol. Chem. 277:27412-22
    • (2002) J. Biol. Chem. , vol.277 , pp. 27412-27422
    • Varnai, P.1    Lin, X.2    Lee, S.B.3    Tuymetova, G.4    Bondeva, T.5
  • 60
    • 0035823602 scopus 로고    scopus 로고
    • G-protein-coupled receptor activation induces the membrane translocation and activation of phosphatidylinositol-4-phosphate 5-kinase Ialpha by a rac- and rho-dependent pathway
    • Chatah NE, Abrams CS. 2001. G-protein-coupled receptor activation induces the membrane translocation and activation of phosphatidylinositol-4- phosphate 5-kinase Ialpha by a rac- and rho-dependent pathway. J. Biol. Chem. 276:34,59-65
    • (2001) J. Biol. Chem. , vol.276 , pp. 3459-3465
    • Chatah, N.E.1    Abrams, C.S.2
  • 61
    • 17144439652 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3
    • Rozelle AL, Machesky LM, Yamamoto M, Driessens MH, Insall RH, et al. 2000. Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3. Curr. Biol. 10:311-20
    • (2000) Curr. Biol. , vol.10 , pp. 311-320
    • Rozelle, A.L.1    Machesky, L.M.2    Yamamoto, M.3    Driessens, M.H.4    Insall, R.H.5
  • 62
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong LD, Traynor-Kaplan A, Bokoch GM, Schwartz MA. 1994. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79:507-13
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 63
    • 0006178818 scopus 로고    scopus 로고
    • Stimulation of phosphatidylinositol-4-phosphate 5-kinase by Rho-kinase
    • Oude Weernink PA, Schulte P, Guo Y, Wetzel J, Amano M, et al. 2000. Stimulation of phosphatidylinositol-4-phosphate 5-kinase by Rho-kinase. J. Biol. Chem. 275:10,168-74
    • (2000) J. Biol. Chem. , vol.275 , pp. 10168-10174
    • Oude Weernink, P.A.1    Schulte, P.2    Guo, Y.3    Wetzel, J.4    Amano, M.5
  • 64
    • 0035809927 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate induces actin stress-fiber formation and inhibits membrane ruffling in CV1 cells
    • Yamamoto M, Hilgemann DH, Feng S, Bito H, Ishihara H, et al. 2001. Phosphatidylinositol 4,5-bisphosphate induces actin stress-fiber formation and inhibits membrane ruffling in CV1 cells. J. Cell Biol. 152:867-76
    • (2001) J. Cell Biol. , vol.152 , pp. 867-876
    • Yamamoto, M.1    Hilgemann, D.H.2    Feng, S.3    Bito, H.4    Ishihara, H.5
  • 65
    • 0033777307 scopus 로고    scopus 로고
    • In vitro interaction of phosphoinositide-4-phosphate 5-kinases with Rac
    • Tolias K, Carpenter CL. 2000. In vitro interaction of phosphoinositide-4-phosphate 5-kinases with Rac. Methods Enzymol. 325:190-200
    • (2000) Methods Enzymol. , vol.325 , pp. 190-200
    • Tolias, K.1    Carpenter, C.L.2
  • 66
    • 0031882760 scopus 로고    scopus 로고
    • Characterization of a Rac1- and RhoGDI-associated lipid kinase signaling complex
    • Tolias KF, Couvillon AD, Cantley LC, Carpenter CL. 1998. Characterization of a Rac1- and RhoGDI-associated lipid kinase signaling complex. Mol. Cell. Biol. 18:762-70
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 762-770
    • Tolias, K.F.1    Couvillon, A.D.2    Cantley, L.C.3    Carpenter, C.L.4
  • 67
    • 0035817625 scopus 로고    scopus 로고
    • Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D
    • Santy LC, Casanova JE. 2001. Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D. J. Cell Biol. 154:599-610
    • (2001) J. Cell Biol. , vol.154 , pp. 599-610
    • Santy, L.C.1    Casanova, J.E.2
  • 68
    • 0035895910 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate 5-kinase type I is regulated through phosphorylation response by extracellular stimuli
    • Park SJ, Itoh T, Takenawa T. 2001. Phosphatidylinositol 4-phosphate 5-kinase type I is regulated through phosphorylation response by extracellular stimuli. J. Biol. Chem. 276:4781-87
    • (2001) J. Biol. Chem. , vol.276 , pp. 4781-4787
    • Park, S.J.1    Itoh, T.2    Takenawa, T.3
  • 69
    • 0037155210 scopus 로고    scopus 로고
    • Mechanism of ARF-stimulated phosphatidylinositol 4,5-bisphosphate synthesis in HL60 cells
    • Skippen A, Jones DH, Morgan CP, Li M, Cockcroft S. 2001. Mechanism of ARF-stimulated phosphatidylinositol 4,5-bisphosphate synthesis in HL60 cells. J. Biol. Chem. 277:5823-31
    • (2001) J. Biol. Chem. , vol.277 , pp. 5823-5831
    • Skippen, A.1    Jones, D.H.2    Morgan, C.P.3    Li, M.4    Cockcroft, S.5
  • 71
    • 0035802108 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic
    • Brown FD, Rozelle AL, Yin HL, Balla T, Donaldson JG. 2001. Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic. J. Cell Biol. 154:1007-18
    • (2001) J. Cell Biol. , vol.154 , pp. 1007-1018
    • Brown, F.D.1    Rozelle, A.L.2    Yin, H.L.3    Balla, T.4    Donaldson, J.G.5
  • 72
    • 0035958955 scopus 로고    scopus 로고
    • Actin directly interacts with phospholipase D, inhibiting its activity
    • Lee S, Park JB; Kim JH, Kim Y, Kim JH, et al. 2001. Actin directly interacts with phospholipase D, inhibiting its activity. J. Biol. Chem. 276:28252-60
    • (2001) J. Biol. Chem. , vol.276 , pp. 28252-28260
    • Lee, S.1    Park, J.B.2    Kim, J.H.3    Kim, Y.4    Kim, J.H.5
  • 74
    • 0034698929 scopus 로고    scopus 로고
    • Two pathways through Cdc42 couple the N-formyl receptor to actin nucleation in permeabilized human neutrophils
    • Glogauer M, Hartwig J, Stossel T. 2000. Two pathways through Cdc42 couple the N-formyl receptor to actin nucleation in permeabilized human neutrophils. J. Cell Biol. 150:785-96
    • (2000) J. Cell Biol. , vol.150 , pp. 785-796
    • Glogauer, M.1    Hartwig, J.2    Stossel, T.3
  • 75
    • 0034633643 scopus 로고    scopus 로고
    • Intracellular delivery of phosphoinositides and inositol phosphates using polyamine carriers
    • Ozaki S, DeWald DB, Shope JC, Chen J, Prestwich GD. 2000. Intracellular delivery of phosphoinositides and inositol phosphates using polyamine carriers. Proc. Natl. Acad. Sci. USA 97:11,286-91
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11
    • Ozaki, S.1    DeWald, D.B.2    Shope, J.C.3    Chen, J.4    Prestwich, G.D.5
  • 76
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate
    • Gilmore AP, Burridge K. 1996. Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate. Nature 381:531-35
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 77
    • 0035951092 scopus 로고    scopus 로고
    • Involvement of phosphatidylinositol 4,5-bisphosphate in phosphatidylserine exposure in platelets: Use of a permeant phosphoinositide- binding peptide
    • Bucki R, Janmey PA, Vegners R, Giraud F, Sulpice JC. 2001. Involvement of phosphatidylinositol 4,5-bisphosphate in phosphatidylserine exposure in platelets: use of a permeant phosphoinositide-binding peptide. Biochemistry 40:15752-61
    • (2001) Biochemistry , vol.40 , pp. 15752-15761
    • Bucki, R.1    Janmey, P.A.2    Vegners, R.3    Giraud, F.4    Sulpice, J.C.5
  • 78
    • 0035900756 scopus 로고    scopus 로고
    • Cell permeant polyphosphoinositide-binding peptides that block cell motility and actin assembly
    • Cunningham CC, Vegners R, Bucki R, Funaki M, Korde N, et al. 2001. Cell permeant polyphosphoinositide-binding peptides that block cell motility and actin assembly. J. Biol. Chem. 276:43390-99
    • (2001) J. Biol. Chem. , vol.276 , pp. 43390-43399
    • Cunningham, C.C.1    Vegners, R.2    Bucki, R.3    Funaki, M.4    Korde, N.5
  • 79
    • 0036473058 scopus 로고    scopus 로고
    • Gelsolin - Evidence for a role in turnover of junction-related actin filaments in Sertoli cells
    • Guttman JA, Janmey P, Vogl AW. 2002. Gelsolin - evidence for a role in turnover of junction-related actin filaments in Sertoli cells. J. Cell Sci. 115:499-505
    • (2002) J. Cell Sci. , vol.115 , pp. 499-505
    • Guttman, J.A.1    Janmey, P.2    Vogl, A.W.3
  • 80
    • 0035881755 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts
    • Caroni P. 2001. Actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts. EMBO J. 20:4332-36
    • (2001) EMBO J. , vol.20 , pp. 4332-4336
    • Caroni, P.1
  • 81
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • Laux T, Fukami K, Thelen M, Golub T, Frey D, Caroni P. 2000. GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. J. Cell Biol. 149:1455-72
    • (2000) J. Cell Biol. , vol.149 , pp. 1455-1472
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 82
    • 0037022127 scopus 로고    scopus 로고
    • Essential role of type I(alpha) phosphatidylinositol 4-phosphate 5-kinase in neurite remodeling
    • van Horck FP, Lavazais E, Eickholt BJ, Moolenaar WH, Divecha N. 2002. Essential role of type I(alpha) phosphatidylinositol 4-phosphate 5-kinase in neurite remodeling. Curr. Biol. 12:241-45
    • (2002) Curr. Biol. , vol.12 , pp. 241-245
    • Van Horck, F.P.1    Lavazais, E.2    Eickholt, B.J.3    Moolenaar, W.H.4    Divecha, N.5
  • 84
    • 0037039414 scopus 로고    scopus 로고
    • From the cover: The large GTPase dynamin regulates actin comet formation and movement in living cells
    • Orth JD, Krueger EW, Cao H, McNiven MA. 2002. From the cover: the large GTPase dynamin regulates actin comet formation and movement in living cells. Proc. Natl. Acad. Sci. USA 99:167-72
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 167-172
    • Orth, J.D.1    Krueger, E.W.2    Cao, H.3    McNiven, M.A.4
  • 86
    • 0034646615 scopus 로고    scopus 로고
    • Identification and characterization of a novel inositol polyphosphate 5-phosphatase
    • Ijuin T, Mochizuki Y, Fukami K, Funaki M, Asano T, Takenawa T. 2000. Identification and characterization of a novel inositol polyphosphate 5-phosphatase. J. Biol. Chem. 275:10,870-75
    • (2000) J. Biol. Chem. , vol.275 , pp. 10
    • Ijuin, T.1    Mochizuki, Y.2    Fukami, K.3    Funaki, M.4    Asano, T.5    Takenawa, T.6
  • 87
    • 0030981640 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments
    • Sakisaka T, Itoh T, Miura K, Takenawa T. 1997. Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments. Mol. Cell. Biol. 17:3841-49
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3841-3849
    • Sakisaka, T.1    Itoh, T.2    Miura, K.3    Takenawa, T.4
  • 88
    • 0034134216 scopus 로고    scopus 로고
    • Ocrl1, a PtdIns(4,5)P(2) 5-phosphatase, is localized to the trans-Golgi network of fibroblasts and epithelial cells
    • Dressman MA, Olivos-Glander IM, Nussbaum RL, Suchy SF. 2000. Ocrl1, a PtdIns(4,5)P(2) 5-phosphatase, is localized to the trans-Golgi network of fibroblasts and epithelial cells. J. Histochem. Cytochem. 48:179-90
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 179-190
    • Dressman, M.A.1    Olivos-Glander, I.M.2    Nussbaum, R.L.3    Suchy, S.F.4
  • 89
    • 0038361129 scopus 로고    scopus 로고
    • Functional overlap between murine Inpp5b and Ocrl1 may explain why deficiency of the murine ortholog for OCRL1 does not cause Lowe syndrome in mice
    • Janne PA, Suchy SF, Bernard D, MacDonald M, Crawley J, et al. 1998. Functional overlap between murine Inpp5b and Ocrl1 may explain why deficiency of the murine ortholog for OCRL1 does not cause Lowe syndrome in mice. J. Clin. Invest. 101:2042-53
    • (1998) J. Clin. Invest. , vol.101 , pp. 2042-2053
    • Janne, P.A.1    Suchy, S.F.2    Bernard, D.3    MacDonald, M.4    Crawley, J.5
  • 90
    • 0031762658 scopus 로고    scopus 로고
    • Skittles, a Drosophila phosphatidylinositol 4-phosphate 5-kinase, is required for cell viability, germline development and bristle morphology, but not for neurotransmitter release
    • Hassan BA, Prokopenko SN, Breuer S, Zhang B, Paululat A, Bellen HJ. 1998. Skittles, a Drosophila phosphatidylinositol 4-phosphate 5-kinase, is required for cell viability, germline development and bristle morphology, but not for neurotransmitter release. Genetics 150:1527-37
    • (1998) Genetics , vol.150 , pp. 1527-1537
    • Hassan, B.A.1    Prokopenko, S.N.2    Breuer, S.3    Zhang, B.4    Paululat, A.5    Bellen, H.J.6
  • 92
    • 0032702258 scopus 로고    scopus 로고
    • Proteins that regulate dynamic actin remodeling in response to membrane signaling
    • Yin HL, Stull JT. 1999. Proteins that regulate dynamic actin remodeling in response to membrane signaling. J. Biol. Chem. 274:32,529-30
    • (1999) J. Biol. Chem. , vol.274 , pp. 32
    • Yin, H.L.1    Stull, J.T.2
  • 93
    • 0035399959 scopus 로고    scopus 로고
    • How is actin polymerization nucleated in vivo?
    • Condeelis J. 2001. How is actin polymerization nucleated in vivo? Trends Cell Biol. 11:288-93
    • (2001) Trends Cell Biol. , vol.11 , pp. 288-293
    • Condeelis, J.1
  • 94
    • 0036130255 scopus 로고    scopus 로고
    • Spatial and temporal regulation of actin polymerization for cytoskeleton formation through Arp2/3 complex and WASP/WAVE proteins
    • Suetsugu S, Miki H, Takenawa T. 2002. Spatial and temporal regulation of actin polymerization for cytoskeleton formation through Arp2/3 complex and WASP/WAVE proteins. Cell Motil. Cytoskeleton 51:113-22
    • (2002) Cell Motil. Cytoskeleton , vol.51 , pp. 113-122
    • Suetsugu, S.1    Miki, H.2    Takenawa, T.3
  • 95
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: Activation by a diverse array of proteins
    • Higgs HN, Pollard TD. 2001. Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70:649-76
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 96
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel TP, Boujemaa R, Pantaloni D, Carlier MF. 1999. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401:613-16
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 97
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin β4
    • Pantaloni D, Carlier M-F. 1993. How profilin promotes actin filament assembly in the presence of thymosin β4. Cell 75:1007-14
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.-F.2
  • 98
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina TM, Borisy GG. 1999. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145:1009-26
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 99
    • 0035969247 scopus 로고    scopus 로고
    • Filamin A, the Arp2/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells
    • Flanagan LA, Chou J, Falet H, Neujahr R, Hartwig JH, Stossel TP. 2001. Filamin A, the Arp2/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells. J. Cell Biol. 155:511-17
    • (2001) J. Cell Biol. , vol.155 , pp. 511-517
    • Flanagan, L.A.1    Chou, J.2    Falet, H.3    Neujahr, R.4    Hartwig, J.H.5    Stossel, T.P.6
  • 100
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • Blanchoin L, Amann KJ, Higgs HN, Marchand JB, Kaiser DA, Pollard TD. 2000. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404:1007-11
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1    Amann, K.J.2    Higgs, H.N.3    Marchand, J.B.4    Kaiser, D.A.5    Pollard, T.D.6
  • 101
    • 0037022632 scopus 로고    scopus 로고
    • Phosphatidylinositol-dependent actin filament binding by the SWI/ SNF-like BAF chromatin remodeling complex
    • Rando OJ, Zhao K, Janmey P, Crabtree GR. 2002. Phosphatidylinositol- dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex. Proc. Natl. Acad. Sci. USA 99:2824-29
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2824-2829
    • Rando, O.J.1    Zhao, K.2    Janmey, P.3    Crabtree, G.R.4
  • 103
    • 0035972165 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the actin filament binding protein Abp1p
    • Goode BL, Rodal AA, Barnes G, Drubin DG. 2001. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J. Cell Biol. 153:627-34
    • (2001) J. Cell Biol. , vol.153 , pp. 627-634
    • Goode, B.L.1    Rodal, A.A.2    Barnes, G.3    Drubin, D.G.4
  • 104
    • 17344380140 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactinactomyosin II complex and malignant transformation
    • He H, Watanabe T, Zhan X, Huang C, Schuuring E, et al. 1998. Role of phosphatidylinositol 4,5-bisphosphate in Ras/ Rac-induced disruption of the cortactinactomyosin II complex and malignant transformation. Mol. Cell Biol. 18:3829-37
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3829-3837
    • He, H.1    Watanabe, T.2    Zhan, X.3    Huang, C.4    Schuuring, E.5
  • 106
    • 0034795423 scopus 로고    scopus 로고
    • N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility
    • Snapper SB, Takeshima F, Anton I, Liu CH, Thomas SM, et al. 2001. N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility. Nat. Cell Biol. 3:897-904
    • (2001) Nat. Cell Biol. , vol.3 , pp. 897-904
    • Snapper, S.B.1    Takeshima, F.2    Anton, I.3    Liu, C.H.4    Thomas, S.M.5
  • 107
    • 0034769365 scopus 로고    scopus 로고
    • Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells
    • Lommel S, Benesch S, Rottner K, Franz T, Wehland J, Kuhn R. 2001. Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2:850-57
    • (2001) EMBO Rep. , vol.2 , pp. 850-857
    • Lommel, S.1    Benesch, S.2    Rottner, K.3    Franz, T.4    Wehland, J.5    Kuhn, R.6
  • 109
    • 0035846598 scopus 로고    scopus 로고
    • Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
    • Zalevsky J, Lempert L, Kranitz H, Mullins RD. 2001. Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities. Curr. Biol. 11:1903-13
    • (2001) Curr. Biol. , vol.11 , pp. 1903-1913
    • Zalevsky, J.1    Lempert, L.2    Kranitz, H.3    Mullins, R.D.4
  • 110
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK. 2000. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404:151-58
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 111
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda KE, Scott JA, Mullins RD, Lim WA. 2000. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290:801-6
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 112
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate
    • Rohatgi R, Ho HY, Kirschner MW. 2000. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate. J. Cell Biol. 150:1299-1310
    • (2000) J. Cell Biol. , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 113
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R, Ma L, Miki H, Lopez M, Kirchhausen T, et al. 1999. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97:221-31
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5
  • 114
    • 0033012399 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein (WASP): Roles in signaling and cytoskeletal organization
    • Snapper SB, Rosen FS. 1999. The Wiskott-Aldrich syndrome protein (WASP): roles in signaling and cytoskeletal organization. Annu. Rev. Immunol. 17:905-29
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 905-929
    • Snapper, S.B.1    Rosen, F.S.2
  • 116
    • 0033780474 scopus 로고    scopus 로고
    • A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization
    • Moreau V, Frischknecht F, Reckmann I, Vincentelli R, Rabut G, et al. 2000. A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nat. Cell Biol. 2:441-48
    • (2000) Nat. Cell Biol. , vol.2 , pp. 441-448
    • Moreau, V.1    Frischknecht, F.2    Reckmann, I.3    Vincentelli, R.4    Rabut, G.5
  • 117
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L, Puntener D, Helenius A. 2002. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296:535-39
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 118
    • 0035901569 scopus 로고    scopus 로고
    • The F-actin side binding activity of the Arp2/3 complex is essential for actin nucleation and lamellipod extension
    • Bailly M, Ichetovkin I, Grant W, Zebda N, Machesky LM, et al. 2001. The F-actin side binding activity of the Arp2/3 complex is essential for actin nucleation and lamellipod extension. Curr. Biol. 11:620-25
    • (2001) Curr. Biol. , vol.11 , pp. 620-625
    • Bailly, M.1    Ichetovkin, I.2    Grant, W.3    Zebda, N.4    Machesky, L.M.5
  • 119
    • 0033529620 scopus 로고    scopus 로고
    • Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase
    • Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, et al. 1999. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285:895-98
    • (1999) Science , vol.285 , pp. 895-898
    • Maekawa, M.1    Ishizaki, T.2    Boku, S.3    Watanabe, N.4    Fujita, A.5
  • 120
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat
    • Edwards DC, Sanders LC, Bokoch GM, Gill GN. 1999. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. 1:253-59
    • (1999) Cell Biol. , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 121
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T. 2002. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108:233-46
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 122
    • 0034722329 scopus 로고    scopus 로고
    • Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension
    • Zebda N, Bernard O, Bailly M, Welti S, Lawrence DS, Condeelis JS. 2000. Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension. J. Cell Biol. 151:1119-28
    • (2000) J. Cell Biol. , vol.151 , pp. 1119-1128
    • Zebda, N.1    Bernard, O.2    Bailly, M.3    Welti, S.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 124
    • 0035951069 scopus 로고    scopus 로고
    • Identification of yeast cofilin residues specific for actin monomer and PIP2 binding
    • Ojala PJ, Paavilainen V, Lappalainen P. 2001. Identification of yeast cofilin residues specific for actin monomer and PIP2 binding. Biochemistry 40:15,562-69
    • (2001) Biochemistry , vol.40 , pp. 15562-15569
    • Ojala, P.J.1    Paavilainen, V.2    Lappalainen, P.3
  • 125
  • 126
    • 0032531960 scopus 로고    scopus 로고
    • Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid
    • Meerschaert K, De Corte V, De Ville Y, Vandekerckhove J, Gettemans J. 1998. Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid. EMBO J. 17:5923-32
    • (1998) EMBO J. , vol.17 , pp. 5923-5932
    • Meerschaert, K.1    De Corte, V.2    De Ville, Y.3    Vandekerckhove, J.4    Gettemans, J.5
  • 127
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig JH, Bokoch GM, Carpenter CL, Janmey PA, Taylor LA, et al. 1995. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82:643-53
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5
  • 128
    • 0029954225 scopus 로고    scopus 로고
    • Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
    • Barkalow K, Witke W, Kwiatkowski DJ, Hartwig JH. 1996. Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J. Cell Biol. 134:389-99
    • (1996) J. Cell Biol. , vol.134 , pp. 389-399
    • Barkalow, K.1    Witke, W.2    Kwiatkowski, D.J.3    Hartwig, J.H.4
  • 130
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke W, Sharpe AH, Hartwig JH, Azuma T, Stossel TP, Kwiatkowski DJ. 1995. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell 81:41-51
    • (1995) Cell , vol.81 , pp. 41-51
    • Witke, W.1    Sharpe, A.H.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 134
    • 0021923779 scopus 로고
    • Diacylglycerol in large alpha-actinin/actin complexes and in the cytoskeleton of activated platelets
    • Burn P, Rotman A, Meyer RK, Burger MM. 1985. Diacylglycerol in large alpha-actinin/actin complexes and in the cytoskeleton of activated platelets. Nature 314:469-72
    • (1985) Nature , vol.314 , pp. 469-472
    • Burn, P.1    Rotman, A.2    Meyer, R.K.3    Burger, M.M.4
  • 135
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function
    • Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, Takenawa T. 1992. Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function. Nature 359:150-52
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 136
    • 0035676002 scopus 로고    scopus 로고
    • Identification of lipids as the main component of skeletal muscle Z-discs
    • Takahashi K, Shimada K, Ahn DH, Ji JR. 2001. Identification of lipids as the main component of skeletal muscle Z-discs. J. Muscle Res. Cell Motil. 22:353-60
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 353-360
    • Takahashi, K.1    Shimada, K.2    Ahn, D.H.3    Ji, J.R.4
  • 138
    • 0024421755 scopus 로고
    • Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin
    • Caldwell JE, Heiss SG, Mermall V, Cooper JA. 1989. Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin. Biochemistry 28:8506-14
    • (1989) Biochemistry , vol.28 , pp. 8506-8514
    • Caldwell, J.E.1    Heiss, S.G.2    Mermall, V.3    Cooper, J.A.4
  • 139
    • 0034835245 scopus 로고    scopus 로고
    • Actin filament assembly and actin-myosin contractility are necessary for anchorage- and EGF-dependent activation of phospholipase Cgamma
    • Suzuki K, Takahashi K. 2001. Actin filament assembly and actin-myosin contractility are necessary for anchorage-and EGF-dependent activation of phospholipase Cgamma. J. Cell Physiol. 189:64-71
    • (2001) J. Cell Physiol. , vol.189 , pp. 64-71
    • Suzuki, K.1    Takahashi, K.2
  • 140
    • 0028050414 scopus 로고
    • Phosphatidylinositol 3-kinase binds to alpha-actinin through the p85 subunit
    • Shibasaki F, Fukami K, Fukui Y, Takenawa T. 1994. Phosphatidylinositol 3-kinase binds to alpha-actinin through the p85 subunit. Biochem. J. 302(Pt 2):551-57
    • (1994) Biochem. J. , vol.302 , Issue.2 PART , pp. 551-557
    • Shibasaki, F.1    Fukami, K.2    Fukui, Y.3    Takenawa, T.4
  • 141
    • 0034685851 scopus 로고    scopus 로고
    • Alpha-Actinin is a potent regulator of G protein-coupled receptor kinase activity and substrate specificity in vitro
    • Freeman JL, Pitcher JA, Li X, Bennett V, Lefkowitz RJ. 2000. alpha-Actinin is a potent regulator of G protein-coupled receptor kinase activity and substrate specificity in vitro. FEBS Lett. 473:280-84
    • (2000) FEBS Lett. , vol.473 , pp. 280-284
    • Freeman, J.L.1    Pitcher, J.A.2    Li, X.3    Bennett, V.4    Lefkowitz, R.J.5
  • 142
    • 0034618121 scopus 로고    scopus 로고
    • Restructuring of focal adhesion plaques by PI 3-kinase. Regulation by PtdIns (3,4,5)-p(3) binding to alpha-actinin
    • Greenwood JA, Theibert AB, Prestwich GD, Murphy -Ullrich JE. 2000. Restructuring of focal adhesion plaques by PI 3-kinase. Regulation by PtdIns (3,4,5)-p(3) binding to alpha-actinin. J. Cell Biol. 150:627-42
    • (2000) J. Cell Biol. , vol.150 , pp. 627-642
    • Greenwood, J.A.1    Theibert, A.B.2    Prestwich, G.D.3    Murphy, J.E.4
  • 143
    • 0034383951 scopus 로고    scopus 로고
    • The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism
    • Young P, Gautel M. 2000. The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism. EMBO J. 19:6331-40
    • (2000) EMBO J. , vol.19 , pp. 6331-6340
    • Young, P.1    Gautel, M.2
  • 144
    • 0026683647 scopus 로고
    • Inositol phospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin
    • Furuhashi K, Inagaki M, Hatano S, Fukami K, Takenawa T. 1992. Inositol phospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin. Biochem. Biophys. Res. Commun. 184:1261-65
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1261-1265
    • Furuhashi, K.1    Inagaki, M.2    Hatano, S.3    Fukami, K.4    Takenawa, T.5
  • 145
    • 0032521369 scopus 로고    scopus 로고
    • Metabolites of the phospholipase D pathway regulate H2O2-induced filamin redistribution in endothelial cells
    • Hastie LE, Patton WF, Hechtman HB, Shepro D. 1998. Metabolites of the phospholipase D pathway regulate H2O2-induced filamin redistribution in endothelial cells. J. Cell Biochem. 68:511-24
    • (1998) J. Cell Biochem. , vol.68 , pp. 511-524
    • Hastie, L.E.1    Patton, W.F.2    Hechtman, H.B.3    Shepro, D.4
  • 146
    • 0034880196 scopus 로고    scopus 로고
    • Phosphorylation of filamin (ABP-280) regulates the binding to the lipid membrane, integrin, and actin
    • Goldmann WH. 2001. Phosphorylation of filamin (ABP-280) regulates the binding to the lipid membrane, integrin, and actin. Cell Biol. Int. 25:805-8
    • (2001) Cell Biol. Int. , vol.25 , pp. 805-808
    • Goldmann, W.H.1
  • 147
    • 0027970371 scopus 로고
    • Insertion of filamin into lipid membranes examined by calorimetry, the film balance technique, and lipid photolabeling
    • Tempel M, Goldmann WH, Dietrich C, Niggli V, Weber T, et al. 1994. Insertion of filamin into lipid membranes examined by calorimetry, the film balance technique, and lipid photolabeling. Biochemistry 33:12,565-72
    • (1994) Biochemistry , vol.33 , pp. 12
    • Tempel, M.1    Goldmann, W.H.2    Dietrich, C.3    Niggli, V.4    Weber, T.5
  • 148
    • 0034633997 scopus 로고    scopus 로고
    • Dynamin is membrane-active: Lipid insertion is induced by phosphoinositides and phosphatidic acid
    • Burger KN, Demel RA, Schmid SL, de Kruijff B. 2000. Dynamin is membrane-active: lipid insertion is induced by phosphoinositides and phosphatidic acid. Biochemistry 39:12485-93
    • (2000) Biochemistry , vol.39 , pp. 12485-12493
    • Burger, K.N.1    Demel, R.A.2    Schmid, S.L.3    De Kruijff, B.4
  • 149
    • 0035842901 scopus 로고    scopus 로고
    • The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin
    • Dyson JM, O'Malley CJ, Becanovic J, Munday AD, Berndt MC, et al. 2001. The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J. Cell Biol. 155:1065-79
    • (2001) J. Cell Biol. , vol.155 , pp. 1065-1079
    • Dyson, J.M.1    O'Malley, C.J.2    Becanovic, J.3    Munday, A.D.4    Berndt, M.C.5
  • 150
    • 0032783917 scopus 로고    scopus 로고
    • Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides
    • Nakamura F, Huang L, Pestonjamasp K, Luna EJ, Furthmayr H. 1999. Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides. Mol. Biol. Cell 10:2669-85
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2669-2685
    • Nakamura, F.1    Huang, L.2    Pestonjamasp, K.3    Luna, E.J.4    Furthmayr, H.5
  • 151
    • 0034722326 scopus 로고    scopus 로고
    • Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP(2)) binding site in the NH(2)-terminal domain of ezrin correlates with its altered cellular distribution
    • Barret C, Roy C, Montcourrier P, Mangeat P, Niggli V. 2000. Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP(2)) binding site in the NH(2)-terminal domain of ezrin correlates with its altered cellular distribution. J. Cell Biol. 151:1067-80
    • (2000) J. Cell Biol. , vol.151 , pp. 1067-1080
    • Barret, C.1    Roy, C.2    Montcourrier, P.3    Mangeat, P.4    Niggli, V.5
  • 152
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M, Sato N, Kondo T, Yonemura S, Monden M, et al. 1996. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J. Cell Biol. 135:37-51
    • (1996) J. Cell Biol. , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5
  • 153
    • 0032555599 scopus 로고    scopus 로고
    • Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5-bisphosphate
    • Heiska L, Alfthan K, Gronholm M, Vilja P, Vaheri A, Carpen O. 1998. Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 273:21893-1900
    • (1998) J. Biol. Chem. , vol.273 , pp. 21893-21900
    • Heiska, L.1    Alfthan, K.2    Gronholm, M.3    Vilja, P.4    Vaheri, A.5    Carpen, O.6
  • 154
    • 0033523986 scopus 로고    scopus 로고
    • Activation of ERM proteins in vivo by Rho involves phosphatidylinositol 4-phosphate 5-kinase and not ROCK kinases
    • Matsui T, Yonemura S, Tsukita SH, Tsukita SA. 1999. Activation of ERM proteins in vivo by Rho involves phosphatidylinositol 4-phosphate 5-kinase and not ROCK kinases. Curr. Biol. 9:1259-62
    • (1999) Curr. Biol. , vol.9 , pp. 1259-1262
    • Matsui, T.1    Yonemura, S.2    Tsukita, S.H.3    Tsukita, S.A.4
  • 155
    • 0033594950 scopus 로고    scopus 로고
    • Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway
    • Gautreau A, Poullet P, Louvard D, Arpin M. 1999. Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway. Proc. Natl. Acad. Sci. USA 96:7300-5
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7300-7305
    • Gautreau, A.1    Poullet, P.2    Louvard, D.3    Arpin, M.4
  • 156
    • 0037155885 scopus 로고    scopus 로고
    • A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting
    • Serrador JM, Vicente-Manzanares M, Calvo J, Barreiro O, Montoya MC, et al. 2002. A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting. J. Biol. Chem. 277:10,400-9
    • (2002) J. Biol. Chem. , vol.277 , pp. 10400-10409
    • Serrador, J.M.1    Vicente-Manzanares, M.2    Calvo, J.3    Barreiro, O.4    Montoya, M.C.5
  • 157
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada K, Shimizu T, Matsui T, Tsukita S, Hakoshima T. 2000. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19:4449-62
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 158
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • Pearson MA, Reczek D, Bretscher A, Karplus PA. 2000. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 101:259-70
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 159
    • 0035912664 scopus 로고    scopus 로고
    • The 2.7 Å crystal structure of the activated FERM domain of moesin: An analysis of structural changes on activation
    • Edwards SD, Keep NH. 2001. The 2.7 Å crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation. Biochemistry 40:7061-68
    • (2001) Biochemistry , vol.40 , pp. 7061-7068
    • Edwards, S.D.1    Keep, N.H.2
  • 160
    • 0035877656 scopus 로고    scopus 로고
    • Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides
    • Martel V, Racaud-Sultan C, Dupe S, Marie C, Paulhe F, et al. 2001. Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides. J. Biol. Chem. 276:21217-27
    • (2001) J. Biol. Chem. , vol.276 , pp. 21217-21227
    • Martel, V.1    Racaud-Sultan, C.2    Dupe, S.3    Marie, C.4    Paulhe, F.5
  • 161
    • 0032559997 scopus 로고    scopus 로고
    • The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate
    • Huttelmaier S, Mayboroda O, Harbeck B, Jarchau T, Jockusch BM, Rudiger M. 1998. The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. Curr. Biol. 8:479-88
    • (1998) Curr. Biol. , vol.8 , pp. 479-488
    • Huttelmaier, S.1    Mayboroda, O.2    Harbeck, B.3    Jarchau, T.4    Jockusch, B.M.5    Rudiger, M.6
  • 162
    • 0033603360 scopus 로고    scopus 로고
    • Polyphosphoinositides inhibit the interaction of vinculin with actin filaments
    • Steimle PA, Hoffert JD, Adey NB, Craig SW. 1999. Polyphosphoinositides inhibit the interaction of vinculin with actin filaments. J. Biol. Chem. 274:18,414-20
    • (1999) J. Biol. Chem. , vol.274 , pp. 18
    • Steimle, P.A.1    Hoffert, J.D.2    Adey, N.B.3    Craig, S.W.4
  • 164
  • 165
    • 0034633937 scopus 로고    scopus 로고
    • The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: Design of a gain-of-function mutant
    • Van Troys M, Dewitte D, Verschelde JL, Goethals M, Vandekerckhove J, Ampe C. 2000. The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: design of a gain-of-function mutant. Biochemistry 39:12,181-89
    • (2000) Biochemistry , vol.39 , pp. 12
    • Van Troys, M.1    Dewitte, D.2    Verschelde, J.L.3    Goethals, M.4    Vandekerckhove, J.5    Ampe, C.6
  • 167
    • 0026542434 scopus 로고
    • Structural changes in profilin accompany its binding to phosphatidylinositol 4,5-bisphosphate
    • Raghunathan V, Mowery P, Rozycki M, Lindberg U, Schutt C. 1992. Structural changes in profilin accompany its binding to phosphatidylinositol 4,5-bisphosphate. FEBS Lett. 297:46-50
    • (1992) FEBS Lett. , vol.297 , pp. 46-50
    • Raghunathan, V.1    Mowery, P.2    Rozycki, M.3    Lindberg, U.4    Schutt, C.5
  • 168
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction: Evidence for the extended lipid anchorage
    • Tuominen EK, Wallace CJ, Kinnunen PK. 2002. Phospholipid-cytochrome c interaction: evidence for the extended lipid anchorage. J. Biol. Chem. 277:8822-26
    • (2002) J. Biol. Chem. , vol.277 , pp. 8822-8826
    • Tuominen, E.K.1    Wallace, C.J.2    Kinnunen, P.K.3
  • 169
    • 0034673931 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate domain inducers promote phospholipid transverse redistribution in biological membranes
    • Bucki R, Giraud F, Sulpice JC. 2000. Phosphatidylinositol 4,5-bisphosphate domain inducers promote phospholipid transverse redistribution in biological membranes. Biochemistry 39:5838-44
    • (2000) Biochemistry , vol.39 , pp. 5838-5844
    • Bucki, R.1    Giraud, F.2    Sulpice, J.C.3
  • 170
    • 0034906945 scopus 로고    scopus 로고
    • ADP ribosylation factor 6 binding to phosphatidylinositol 4,5-bisphosphate-containing vesicles creates defects in the bilayer structure: An electron spin resonance study
    • Ge M, Cohen JS, Brown HA, Freed JH. 2001. ADP ribosylation factor 6 binding to phosphatidylinositol 4,5-bisphosphate-containing vesicles creates defects in the bilayer structure: an electron spin resonance study. Biophys. J. 81:994-1005
    • (2001) Biophys. J. , vol.81 , pp. 994-1005
    • Ge, M.1    Cohen, J.S.2    Brown, H.A.3    Freed, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.