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Volumn 398, Issue 1, 2006, Pages 1-13

Supervised membrane swimming: Small G-protein lifeguards regulate PIPK signaling and monitor intracellular PtdIns(4,5)P2 pools

Author keywords

ADP ribosylation factor 1 6 (Arf1 Arf6); Phosphatidic acid; Phosphatidylinositol phosphate kinase (PIPK); PtdIns(4,5)P2; Rho Rac Cdc42; Small G protein

Indexed keywords

BACTERIA; BIOELECTRIC POTENTIALS; CELLS; MOLECULAR DYNAMICS; PROTEINS;

EID: 33747184318     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060565     Document Type: Review
Times cited : (85)

References (159)
  • 1
    • 28444482087 scopus 로고    scopus 로고
    • Regulation of protein activities by phosphoinositide phosphates
    • Niggli, V. (2005) Regulation of protein activities by phosphoinositide phosphates. Annu. Rev. Cell Dev. Biol. 21, 57-79
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 57-79
    • Niggli, V.1
  • 2
    • 0035656919 scopus 로고    scopus 로고
    • 2, and cell movement: Similar messages, different meanings?
    • 2, and cell movement: similar messages, different meanings? Dev. Cell 1, 743-747
    • (2001) Dev. Cell , vol.1 , pp. 743-747
    • Insall, R.H.1    Weiner, O.D.2
  • 3
    • 18244376864 scopus 로고    scopus 로고
    • The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKIα
    • Kisseleva, M., Feng, Y., Ward, M., Song, C., Anderson, R. A. and Longmore, G. D. (2005) The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKIα. Mol. Cell. Biol. 25, 3956-3966
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3956-3966
    • Kisseleva, M.1    Feng, Y.2    Ward, M.3    Song, C.4    Anderson, R.A.5    Longmore, G.D.6
  • 4
    • 17644412381 scopus 로고    scopus 로고
    • 2-dependent microdomain assemblies capture microtubules to promote and control leading edge motility
    • 2-dependent microdomain assemblies capture microtubules to promote and control leading edge motility. J. Cell Biol. 169, 151-165
    • (2005) J. Cell Biol. , vol.169 , pp. 151-165
    • Golub, T.1    Caroni, P.2
  • 6
    • 20444428008 scopus 로고    scopus 로고
    • Regulation of ion channels by phosphatidylinositol 4,5-bisphosphate
    • Suh, B. C. and Hille, B. (2005) Regulation of ion channels by phosphatidylinositol 4,5-bisphosphate. Curr. Opin. Neurobiol. 15, 370-378
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 370-378
    • Suh, B.C.1    Hille, B.2
  • 7
    • 0041475820 scopus 로고    scopus 로고
    • ARF6 regulates a plasma membrane pool of phosphatidylinositol(4,5) bisphosphate required for regulated exocytosis
    • Aikawa, Y. and Martin, T. F. (2003) ARF6 regulates a plasma membrane pool of phosphatidylinositol(4,5)bisphosphate required for regulated exocytosis. J. Cell Biol. 162, 647-659
    • (2003) J. Cell Biol. , vol.162 , pp. 647-659
    • Aikawa, Y.1    Martin, T.F.2
  • 9
    • 20444486130 scopus 로고    scopus 로고
    • The activation of exocytotic sites by the formation of phosphatidylinositol 4,5-bisphosphate microdomains at syntaxin clusters
    • Aoyagi, K., Sugaya, I., Umeda, M., Yamamoto, S., Terakawa, S. and Takahashi, M. (2005) The activation of exocytotic sites by the formation of phosphatidylinositol 4,5-bisphosphate microdomains at syntaxin clusters. J. Biol. Chem. 280, 17346-17352
    • (2005) J. Biol. Chem. , vol.280 , pp. 17346-17352
    • Aoyagi, K.1    Sugaya, I.2    Umeda, M.3    Yamamoto, S.4    Terakawa, S.5    Takahashi, M.6
  • 10
    • 0035424240 scopus 로고    scopus 로고
    • 2 regulation of surface membrane traffic
    • 2 regulation of surface membrane traffic. Curr. Opin. Cell Biol. 13, 493-499
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 11
    • 18044364473 scopus 로고    scopus 로고
    • Probing phosphoinositide functions in signaling and membrane trafficking
    • Downes, C. P., Gray, A. and Lucocq, J. M. (2005) Probing phosphoinositide functions in signaling and membrane trafficking. Trends Cell Biol. 15, 259-268
    • (2005) Trends Cell Biol. , vol.15 , pp. 259-268
    • Downes, C.P.1    Gray, A.2    Lucocq, J.M.3
  • 12
    • 0030721527 scopus 로고    scopus 로고
    • A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate
    • Rameh, L. E., Tolias, K. F., Duckworth, B. C. and Cantley, L. C. (1997) A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature (London) 390, 192-196
    • (1997) Nature (London) , vol.390 , pp. 192-196
    • Rameh, L.E.1    Tolias, K.F.2    Duckworth, B.C.3    Cantley, L.C.4
  • 14
    • 0029795811 scopus 로고    scopus 로고
    • Cloning of cDNAs encoding two isoforms of 68-kDa type I phosphatidylinositol-4-phosphate 5-kinase
    • Ishihara, H., Shibasaki, Y., Kizuki, N., Katagiri, H., Yazaki, Y., Asano, T. and Oka, Y. (1996) Cloning of cDNAs encoding two isoforms of 68-kDa type I phosphatidylinositol-4-phosphate 5-kinase. J. Biol. Chem. 271, 23611-23614
    • (1996) J. Biol. Chem. , vol.271 , pp. 23611-23614
    • Ishihara, H.1    Shibasaki, Y.2    Kizuki, N.3    Katagiri, H.4    Yazaki, Y.5    Asano, T.6    Oka, Y.7
  • 15
    • 16944365378 scopus 로고    scopus 로고
    • Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family
    • Loijens, J. C. and Anderson, R. A. (1996) Type I phosphatidylinositol-4- phosphate 5-kinases are distinct members of this novel lipid kinase family. J. Biol. Chem. 271, 32937-32943
    • (1996) J. Biol. Chem. , vol.271 , pp. 32937-32943
    • Loijens, J.C.1    Anderson, R.A.2
  • 16
    • 0032502721 scopus 로고    scopus 로고
    • Type I phosphatidylinositol-4-phosphate 5-kinases: Cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family
    • Ishihara, H., Shibasaki, Y., Kizuki, N., Wada, T., Yazaki, Y., Asano, T. and Oka, Y. (1998) Type I phosphatidylinositol-4-phosphate 5-kinases: cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family. J. Biol. Chem. 273, 8741-8748
    • (1998) J. Biol. Chem. , vol.273 , pp. 8741-8748
    • Ishihara, H.1    Shibasaki, Y.2    Kizuki, N.3    Wada, T.4    Yazaki, Y.5    Asano, T.6    Oka, Y.7
  • 17
    • 0032493744 scopus 로고    scopus 로고
    • A novel phosphatidylinositol-5-phosphate 4-kinase (phosphatidylinositol- phosphate kinase IIγ) is phosphorylated in the endoplasmic reticulum in response to mitogenic signals
    • Itoh, T., Ijuin, T. and Takenawa, T. (1998) A novel phosphatidylinositol- 5-phosphate 4-kinase (phosphatidylinositol-phosphate kinase IIγ) is phosphorylated in the endoplasmic reticulum in response to mitogenic signals. J. Biol. Chem. 273, 20292-20299
    • (1998) J. Biol. Chem. , vol.273 , pp. 20292-20299
    • Itoh, T.1    Ijuin, T.2    Takenawa, T.3
  • 18
    • 0031771547 scopus 로고    scopus 로고
    • Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing pre-mRNA processing factors
    • Boronenkov, I. V., Loijens, J. C., Umeda, M. and Anderson, R. A. (1998) Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing pre-mRNA processing factors. Mol. Biol. Cell 9, 3547-3560
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3547-3560
    • Boronenkov, I.V.1    Loijens, J.C.2    Umeda, M.3    Anderson, R.A.4
  • 19
    • 0033969444 scopus 로고    scopus 로고
    • The activation loop of phosphatidylinositol phosphate kinases determines signaling specificity
    • Kunz, J., Wilson, M. P., Kisseleva, M., Hurley, J. H., Majerus, P. W. and Anderson, R. A. (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
  • 20
    • 0038603841 scopus 로고    scopus 로고
    • Membrane ruffling requires coordination between type Iα phosphatidylinositol phosphate kinase and Rac signaling
    • Doughman, R. L., Firestone, A. J., Wojtasiak, M. L., Bunce, M. W. and Anderson, R. A. (2003) Membrane ruffling requires coordination between type Iα phosphatidylinositol phosphate kinase and Rac signaling. J. Biol. Chem. 278, 23036-23045
    • (2003) J. Biol. Chem. , vol.278 , pp. 23036-23045
    • Doughman, R.L.1    Firestone, A.J.2    Wojtasiak, M.L.3    Bunce, M.W.4    Anderson, R.A.5
  • 21
    • 4644300280 scopus 로고    scopus 로고
    • Regulation and cellular roles of phosphoinositide 5-kinases
    • Oude Weernink, P. A., Schmidt, M. and Jakobs, K. H. (2004) Regulation and cellular roles of phosphoinositide 5-kinases. Eur. J. Pharmacol. 500, 87-99
    • (2004) Eur. J. Pharmacol. , vol.500 , pp. 87-99
    • Oude Weernink, P.A.1    Schmidt, M.2    Jakobs, K.H.3
  • 22
    • 4744370340 scopus 로고    scopus 로고
    • Rho and Rho-kinase mediate thrombin-induced phosphatidylinositol 4-phosphate 5-kinase trafficking in platelets
    • Yang, S. A., Carpenter, C. L. and Abrams, C. S. (2004) Rho and Rho-kinase mediate thrombin-induced phosphatidylinositol 4-phosphate 5-kinase trafficking in platelets. J. Biol. Chem. 279, 42331-42336
    • (2004) J. Biol. Chem. , vol.279 , pp. 42331-42336
    • Yang, S.A.1    Carpenter, C.L.2    Abrams, C.S.3
  • 25
    • 0028346383 scopus 로고
    • Type I phosphatidylinositol 4-phosptiate 5-kinase isoforms are specifically stimulated by phosphatidic acid
    • Jenkins, G. H., Fisette, P. L. and Anderson, R. A. (1994) Type I phosphatidylinositol 4-phosptiate 5-kinase isoforms are specifically stimulated by phosphatidic acid. J. Biol. Chem. 269, 11547-11554
    • (1994) J. Biol. Chem. , vol.269 , pp. 11547-11554
    • Jenkins, G.H.1    Fisette, P.L.2    Anderson, R.A.3
  • 26
    • 0034616881 scopus 로고    scopus 로고
    • Type Iα phosphatidylinositol 4-phosphate 5-kinase is a putative target for increased intracellular phosphatidic acid
    • Jones, D. R., Sanjuan, M. A. and Merida, I. (2000) Type Iα phosphatidylinositol 4-phosphate 5-kinase is a putative target for increased intracellular phosphatidic acid. FEBS Lett. 476, 160-165
    • (2000) FEBS Lett. , vol.476 , pp. 160-165
    • Jones, D.R.1    Sanjuan, M.A.2    Merida, I.3
  • 27
    • 0034676003 scopus 로고    scopus 로고
    • Interaction of the type to PIPkinase with phospholipase D: A role for the local generation of phosphatidylinositol 4,5-bisphosphate in the regulation of PLD2 activity
    • Divecha, N., Roefs, M., Halstead, J. R., D'Andrea, S., Fernandez-Borga, M., Oomen, L., Saqib, K. M., Wakelam, M. J. and D'Santos, C. (2000) Interaction of the type to PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4,5-bisphosphate in the regulation of PLD2 activity. EMBO J. 19, 5440-5449
    • (2000) EMBO J. , vol.19 , pp. 5440-5449
    • Divecha, N.1    Roefs, M.2    Halstead, J.R.3    D'Andrea, S.4    Fernandez-Borga, M.5    Oomen, L.6    Saqib, K.M.7    Wakelam, M.J.8    D'Santos, C.9
  • 28
    • 0037201953 scopus 로고    scopus 로고
    • The regulation of phospholipase D by inositol phospholipids and small GTPases
    • Powner, D. J. and Wakelam, M. J. (2002) The regulation of phospholipase D by inositol phospholipids and small GTPases. FEBS Lett. 531, 62-64
    • (2002) FEBS Lett. , vol.531 , pp. 62-64
    • Powner, D.J.1    Wakelam, M.J.2
  • 29
    • 23744489638 scopus 로고    scopus 로고
    • Phospholipase D2 stimulates integrin-mediated adhesion via phosphatidylinositol 4-phosphate 5-kinase Iγb
    • Powner, D. J., Payne, R. M., Pettitt, T. R., Giudici, M. L., Irvine, R. F. and Wakelam, M. J. (2005) Phospholipase D2 stimulates integrin-mediated adhesion via phosphatidylinositol 4-phosphate 5-kinase Iγb. J. Cell Sci. 118, 2975-2986
    • (2005) J. Cell Sci. , vol.118 , pp. 2975-2986
    • Powner, D.J.1    Payne, R.M.2    Pettitt, T.R.3    Giudici, M.L.4    Irvine, R.F.5    Wakelam, M.J.6
  • 30
    • 0037038412 scopus 로고    scopus 로고
    • Type Iγ phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling, K., Doughman, R. L., Firestone, A. J., Bunce, M. W. and Anderson, R. A. (2002) Type Iγ phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature (London) 420, 89-93
    • (2002) Nature (London) , vol.420 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2    Firestone, A.J.3    Bunce, M.W.4    Anderson, R.A.5
  • 32
    • 32044435884 scopus 로고    scopus 로고
    • Isoprenylated proteins
    • McTaggart, S. J. (2006) Isoprenylated proteins. Cell. Mol. Life Sci. 63, 255-267
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 255-267
    • McTaggart, S.J.1
  • 33
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F. L. and Casey, P. J. (1996) Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65, 241-269
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 34
    • 27944445790 scopus 로고    scopus 로고
    • CZH proteins: A new family of Rho-GEFs
    • Meller, N., Merlot, S. and Guda, C. (2005) CZH proteins: a new family of Rho-GEFs. J. Cell Sci. 118, 4937-4946
    • (2005) J. Cell Sci. , vol.118 , pp. 4937-4946
    • Meller, N.1    Merlot, S.2    Guda, C.3
  • 35
    • 0942279704 scopus 로고    scopus 로고
    • Structural elements, mechanism, and evolutionary convergence of Rho protein-guanine nucleotide exchange factor complexes
    • Erickson, J. W. and Cerione, R. A. (2004) Structural elements, mechanism, and evolutionary convergence of Rho protein-guanine nucleotide exchange factor complexes. Biochemistry 43, 837-842
    • (2004) Biochemistry , vol.43 , pp. 837-842
    • Erickson, J.W.1    Cerione, R.A.2
  • 36
    • 0037213689 scopus 로고    scopus 로고
    • Rho GTPase-activating proteins in cell regulation
    • Moon, S. Y. and Zheng, Y. (2003) Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 13, 13-22
    • (2003) Trends Cell Biol. , vol.13 , pp. 13-22
    • Moon, S.Y.1    Zheng, Y.2
  • 37
    • 23944518413 scopus 로고    scopus 로고
    • RhoGDI: Multiple functions in the regulation of Rho family GTPase activities
    • Dovas, A. and Couchman, J. R. (2005) RhoGDI: multiple functions in the regulation of Rho family GTPase activities. Biochem. J. 390, 1-9
    • (2005) Biochem. J. , vol.390 , pp. 1-9
    • Dovas, A.1    Couchman, J.R.2
  • 38
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K. and Wennerberg, K. (2004) Rho and Rac take center stage. Cell 116, 167-179
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 39
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt, A. and Hall, A. (2002) Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16, 1587-1609
    • (2002) Genes Dev. , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 42
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K. F., Cantley, L. C. and Carpenter, C. L. (1995) Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270, 17656-17659
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 43
    • 0030944208 scopus 로고    scopus 로고
    • Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate
    • Randazzo, P. A. (1997) Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 272, 7688-7692
    • (1997) J. Biol. Chem. , vol.272 , pp. 7688-7692
    • Randazzo, P.A.1
  • 44
    • 0034673998 scopus 로고    scopus 로고
    • Binding of the PH and polybasic C-terminal domains of ARNO to phosphoinositides and to acidic lipids
    • Macia, E., Paris, S. and Chabre, M. (2000) Binding of the PH and polybasic C-terminal domains of ARNO to phosphoinositides and to acidic lipids. Biochemistry 39, 5893-5901
    • (2000) Biochemistry , vol.39 , pp. 5893-5901
    • Macia, E.1    Paris, S.2    Chabre, M.3
  • 45
    • 1842416568 scopus 로고    scopus 로고
    • Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno
    • Paris, S., Beraud-Dufour, S., Robineau, S., Bigay, J., Antonny, B., Chabre, M. and Chardin, P. (1997) Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno. J. Biol. Chem. 272, 22221-22226
    • (1997) J. Biol. Chem. , vol.272 , pp. 22221-22226
    • Paris, S.1    Beraud-Dufour, S.2    Robineau, S.3    Bigay, J.4    Antonny, B.5    Chabre, M.6    Chardin, P.7
  • 46
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J. and Hall, A. (1992) The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 47
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L. D., Traynor-Kaplan, A., Bokoch, G. M. and Schwartz, M. A. (1994) The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79, 507-513
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 50
    • 0030063978 scopus 로고    scopus 로고
    • Inhibition of receptor signaling to phospholipase D by Clostridium difficile toxin B: Role of Rho proteins
    • Schmidt, M., Rumenapp, U., Bienek, C., Keller, J., von Eichel-Streiber, C. and Jakobs, K. H. (1996) Inhibition of receptor signaling to phospholipase D by Clostridium difficile toxin B: role of Rho proteins. J. Biol. Chem. 271, 2422-2426
    • (1996) J. Biol. Chem. , vol.271 , pp. 2422-2426
    • Schmidt, M.1    Rumenapp, U.2    Bienek, C.3    Keller, J.4    Von Eichel-Streiber, C.5    Jakobs, K.H.6
  • 51
    • 0030001638 scopus 로고    scopus 로고
    • Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
    • Ren, X. D., Bokoch, G. M., Traynor-Kaplan, A., Jenkins, G. H., Anderson, R. A. and Schwartz, M. A. (1996) Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol. Biol. Cell 7, 435-442
    • (1996) Mol. Biol. Cell , vol.7 , pp. 435-442
    • Ren, X.D.1    Bokoch, G.M.2    Traynor-Kaplan, A.3    Jenkins, G.H.4    Anderson, R.A.5    Schwartz, M.A.6
  • 53
    • 0035809927 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate induces actin stress-fiber formation and inhibits membrane ruffling in CV1 cells
    • Yamamoto, M., Hilgemann, D. H., Feng, S., Bito, H., Ishihara, H., Shibasaki, Y. and Yin, H. L. (2001) Phosphatidylinositol 4,5-bisphosphate induces actin stress-fiber formation and inhibits membrane ruffling in CV1 cells. J. Cell Biol. 152, 867-876
    • (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    Shibasaki, Y.6    Yin, H.L.7
  • 54
    • 0035930528 scopus 로고    scopus 로고
    • Differential regulation of Rho and Rac through heterotrimeric G-proteins and cyclic nucleotides
    • Gratacap, M. P., Payrastre, B., Nieswandt, B. and Offermanns, S. (2001) Differential regulation of Rho and Rac through heterotrimeric G-proteins and cyclic nucleotides. J. Biol. Chem. 276, 47906-47913
    • (2001) J. Biol. Chem. , vol.276 , pp. 47906-47913
    • Gratacap, M.P.1    Payrastre, B.2    Nieswandt, B.3    Offermanns, S.4
  • 56
  • 57
    • 0033523986 scopus 로고    scopus 로고
    • Activation of ERM proteins in vivo by Rho involves phosphatidyl-inositol 4-phosphate 5-kinase and not ROCK kinases
    • Matsui, T., Yonemura, S., Tsukita, S. and Tsukita, S. (1999) Activation of ERM proteins In vivo by Rho involves phosphatidyl-inositol 4-phosphate 5-kinase and not ROCK kinases. Curr. Biol. 9, 1259-1262
    • (1999) Curr. Biol. , vol.9 , pp. 1259-1262
    • Matsui, T.1    Yonemura, S.2    Tsukita, S.3    Tsukita, S.4
  • 58
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: Integrators at the cell cortex
    • Bretscher, A., Edwards, K. and Fehon, R. G. (2002) ERM proteins and merlin: integrators at the cell cortex. Nat. Rev. Mol. Cell Biol. 3, 586-599
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 59
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D. and Hall, A. (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70, 401-410
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 60
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science 279, 509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 61
    • 0031882760 scopus 로고    scopus 로고
    • Characterization of a Rac1- and RhoGDI-associated lipid kinase signaling complex
    • Tolias, K. F., Couvillon, A. D., Cantley, L. C. and Carpenter, C. L. (1998) Characterization of a Rac1- and RhoGDI-associated lipid kinase signaling complex. Mol. Cell. Biol. 18, 762-770
    • (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
  • 64
    • 1542319943 scopus 로고    scopus 로고
    • Activation of type I phosphatidylinositol 4-phosphate 5-kinase isoforms by the Rho GTPases, RhoA, Rac1, and Cdc42
    • Weernink, P. A., Meletiadis, K., Hommeltenberg, S., Hinz, M., Ishihara, H., Schmidt, M. and Jakobs, K. H. (2004) Activation of type I phosphatidylinositol 4-phosphate 5-kinase isoforms by the Rho GTPases, RhoA, Rac1, and Cdc42. J. Biol. Chem. 279, 7840-7849
    • (2004) J. Biol. Chem. , vol.279 , pp. 7840-7849
    • Weernink, P.A.1    Meletiadis, K.2    Hommeltenberg, S.3    Hinz, M.4    Ishihara, H.5    Schmidt, M.6    Jakobs, K.H.7
  • 65
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., Bokoch, G. M., Carpenter, C. L., Janmey, P. A., Taylor, L. A., Toker, A. and Stossel, T. P. (1995) Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82, 643-653
    • (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    Toker, A.6    Stossel, T.P.7
  • 67
    • 0035823602 scopus 로고    scopus 로고
    • G-protein-coupled receptor activation induces the membrane translocation and activation of phosphatidylinositol-4-phosphate 5-kinase Iα by a Rac- and Rho-dependent pathway
    • Chatah, N. E. and Abrams, C. S. (2001) G-protein-coupled receptor activation induces the membrane translocation and activation of phosphatidylinositol-4-phosphate 5-kinase Iα by a Rac- and Rho-dependent pathway. J. Biol. Chem. 276, 34059-34065
    • (2001) J. Biol. Chem. , vol.276 , pp. 34059-34065
    • Chatah, N.E.1    Abrams, C.S.2
  • 68
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., Ahmed, S., Best, A. and Lim, L. (1995) The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15, 1942-1952
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 69
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D. and Hall, A. (1995) Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 70
    • 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., Takenawa, T. and Kirschner, M. W. (1999) The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 72
    • 0035802108 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic
    • Brown, F. D., Rozelle, A. L., Yin, H. L., Balla, T. and Donaldson, J. G. (2001) Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic. J. Cell Biol. 154, 1007-1017
    • (2001) J. Cell Biol. , vol.154 , pp. 1007-1017
    • Brown, F.D.1    Rozelle, A.L.2    Yin, H.L.3    Balla, T.4    Donaldson, J.G.5
  • 73
    • 0142211351 scopus 로고    scopus 로고
    • Multiple roles for Arf6: Sorting, structuring, and signaling at the plasma membrane
    • Donaldson, J. G. (2003) Multiple roles for Arf6: sorting, structuring, and signaling at the plasma membrane. J. Biol. Chem. 278, 41573-41576
    • (2003) J. Biol. Chem. , vol.278 , pp. 41573-41576
    • Donaldson, J.G.1
  • 74
    • 23844548266 scopus 로고    scopus 로고
    • Localization and function of Art family GTPases
    • Donaldson, J. G. and Honda, A. (2005) Localization and function of Art family GTPases. Biochem. Soc. Trans. 33, 639-642
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 639-642
    • Donaldson, J.G.1    Honda, A.2
  • 75
    • 0035980759 scopus 로고    scopus 로고
    • Phospnoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane
    • Takenavra, T. and Itoh, T. (2001) Phospnoinositides, 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
    • Takenavra, T.1    Itoh, T.2
  • 76
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown, H. A., Gutowski, S., Moomaw, C. R., Slaughter, C. and Sternweis, P. C. (1993) ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 75, 1137-1144
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 78
    • 0033937941 scopus 로고    scopus 로고
    • Regulators and effectors of the ARF GTPases
    • Donaldson, J. G. and Jackson, C. L. (2000) Regulators and effectors of the ARF GTPases. Curr. Opin. Cell Biol. 12, 475-482
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 475-482
    • Donaldson, J.G.1    Jackson, C.L.2
  • 79
    • 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, D. H., Morris, J. B., Morgan, C. P., Kondo, H., Irvine, R. F. and 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, 13962-13966
    • (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
  • 81
    • 0037155210 scopus 로고    scopus 로고
    • Mechanism of ADP ribosylation factor-stimulated phosphatidylinositol 4,5-bisphosphate synthesis in HL60 cells
    • Skippen, A., Jones, D. H., Morgan, C. P., Li, M. and Cockcroft, S. (2002) Mechanism of ADP ribosylation factor-stimulated phosphatidylinositol 4,5-bisphosphate synthesis in HL60 cells. J. Biol. Chem. 277, 5823-5831
    • (2002) 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
  • 82
    • 0345687169 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 regulates insulin secretion through plasma membrane phosphatidylinositol 4,5-bisphosphate
    • Lawrence, J. T. and Birnbaum, M. J. (2003) ADP-ribosylation factor 6 regulates insulin secretion through plasma membrane phosphatidylinositol 4,5-bisphosphate. Proc. Natl. Acad. Sci. U.S.A. 100, 13320-13325
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13320-13325
    • Lawrence, J.T.1    Birnbaum, M.J.2
  • 83
    • 0032900498 scopus 로고    scopus 로고
    • ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements
    • Radrakrishna, H., Al-Awar, O., Khachikian, Z. and Donaldson, J. G. (1999) ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell Sci. 112, 855-866
    • (1999) J. Cell Sci. , vol.112 , pp. 855-866
    • Radrakrishna, H.1    Al-Awar, O.2    Khachikian, Z.3    Donaldson, J.G.4
  • 84
    • 0035817625 scopus 로고    scopus 로고
    • Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D
    • Santy, L. C. and Casanova, J. E. (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
  • 85
    • 0033560032 scopus 로고    scopus 로고
    • EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization
    • Franco, M., Peters, P. J., Boretto, J., van Donselaar, E., Neri, A., D'Souza-Schorey, C. and Chavrier, P. (1999) EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization. EMBO J. 18, 1480-1491
    • (1999) EMBO J. , vol.18 , pp. 1480-1491
    • Franco, M.1    Peters, P.J.2    Boretto, J.3    Van Donselaar, E.4    Neri, A.5    D'Souza-Schorey, C.6    Chavrier, P.7
  • 86
    • 0038825177 scopus 로고    scopus 로고
    • ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Iγ
    • Krauss, M., Kinuta, M., Wenk, M. R., De Camilli, P., Takei, K. and Haucke, V. (2003) ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Iγ. J. Cell Biol. 162, 113-124
    • (2003) J. Cell Biol. , vol.162 , pp. 113-124
    • Krauss, M.1    Kinuta, M.2    Wenk, M.R.3    De Camilli, P.4    Takei, K.5    Haucke, V.6
  • 87
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin, H. L. and Janmey, P. A. (2003) Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol. 65, 761-789
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 88
    • 2942718545 scopus 로고    scopus 로고
    • PI-loting membrane traffic
    • De Matteis, M. A. and Godi, A. (2004) PI-loting membrane traffic. Nat. Cell Biol. 6, 487-492
    • (2004) Nat. Cell Biol. , vol.6 , pp. 487-492
    • De Matteis, M.A.1    Godi, A.2
  • 89
    • 2942623783 scopus 로고    scopus 로고
    • Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: Insights from vesicle recycling in nerve terminals
    • Wenk, M. R. and De Camilli, P. (2004) Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: insights from vesicle recycling in nerve terminals. Proc. Natl. Acad. Sci. U.S.A. 101, 8262-8269
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 8262-8269
    • Wenk, M.R.1    De Camilli, P.2
  • 90
    • 0346729933 scopus 로고    scopus 로고
    • ARNO and ARF6 regulate axonal elongation and branching through downstream activation of phosphatidylinositol 4-phosphate 5-kinase α
    • Hernandez-Deviez, D. J., Roth, M. G., Casanova, J. E. and Wilson, J. M. (2004) ARNO and ARF6 regulate axonal elongation and branching through downstream activation of phosphatidylinositol 4-phosphate 5-kinase α. Mol. Biol. Cell 15 111-120
    • (2004) Mol. Biol. Cell , vol.15 , pp. 111-120
    • Hernandez-Deviez, D.J.1    Roth, M.G.2    Casanova, J.E.3    Wilson, J.M.4
  • 91
    • 0042422047 scopus 로고    scopus 로고
    • Arf6 and phosphoinositol-4-phosphate-5-kinase activities permit bypass of the Rad requirement for β1 integrin-mediated bacterial uptake
    • Wong, K. W. and Isberg, R. R. (2003) Arf6 and phosphoinositol-4- phosphate-5-kinase activities permit bypass of the Rad requirement for β1 integrin-mediated bacterial uptake. J. Exp. Med. 198, 603-614
    • (2003) J. Exp. Med. , vol.198 , pp. 603-614
    • Wong, K.W.1    Isberg, R.R.2
  • 94
    • 0035881755 scopus 로고    scopus 로고
    • 2 rafts
    • 2 rafts. EMBO J. 20, 4332-4336
    • (2001) EMBO J. , vol.20 , pp. 4332-4336
    • Caroni, P.1
  • 96
    • 0025214940 scopus 로고
    • Polyphosphoinositide synthesis in platelets stimulated with low concentrations of thrombin is enhanced before the activation of phospholipase C
    • Lassing, I. and Lindberg, U. (1990) Polyphosphoinositide synthesis in platelets stimulated with low concentrations of thrombin is enhanced before the activation of phospholipase C. FEBS Lett. 262, 231-233
    • (1990) FEBS Lett. , vol.262 , pp. 231-233
    • Lassing, I.1    Lindberg, U.2
  • 97
    • 0025925359 scopus 로고
    • Interaction of pp60c-src, phospholipase C, inositol-lipid, and diacyglycerol kinases with the cytoskeletons of thrombin-stimulated platelets
    • Grondin, P., Plantavid, M., Sultan, C., Breton, M., Mauco, G. and Chap, H. (1991) Interaction of pp60c-src, phospholipase C, inositol-lipid, and diacyglycerol kinases with the cytoskeletons of thrombin-stimulated platelets. J. Biol. Chem. 266, 15705-15709
    • (1991) J. Biol. Chem. , vol.266 , pp. 15705-15709
    • Grondin, P.1    Plantavid, M.2    Sultan, C.3    Breton, M.4    Mauco, G.5    Chap, H.6
  • 98
    • 0029827247 scopus 로고    scopus 로고
    • Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton
    • Hinchliffe, K. A., Irvine, R. F. and Divecha, N. (1996) Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton. EMBO J. 15, 6516-6524
    • (1996) EMBO J. , vol.15 , pp. 6516-6524
    • Hinchliffe, K.A.1    Irvine, R.F.2    Divecha, N.3
  • 99
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: Activation by a diverse array of proteins
    • Higgs, H. N. and Pollard, T. D. (2001) Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70, 649-676
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 100
    • 0034983715 scopus 로고    scopus 로고
    • WASP and WAVE family proteins: Key molecules for rapid rearrangement of cortical actin filaments and cell movement
    • Takenawa, T. and Miki, H. (2001) WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement. J. Cell Sci. 114, 1801-1809
    • (2001) J. Cell Sci. , vol.114 , pp. 1801-1809
    • Takenawa, T.1    Miki, H.2
  • 101
    • 0034142240 scopus 로고    scopus 로고
    • Activation of the small GTPases, rac and cdc42, after ligation of the platelet PAR-1 receptor
    • Azim, A. C., Barkalow, K., Chou, J. and Hartwig, J. H. (2000) Activation of the small GTPases, rac and cdc42, after ligation of the platelet PAR-1 receptor. Blood 95, 959-964
    • (2000) Blood , vol.95 , pp. 959-964
    • Azim, A.C.1    Barkalow, K.2    Chou, J.3    Hartwig, J.H.4
  • 102
    • 0034603198 scopus 로고    scopus 로고
    • Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
    • Hoffman, G. R., Nassar, N. and Cerione, R. A. (2000) Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell 100, 345-356
    • (2000) Cell , vol.100 , pp. 345-356
    • Hoffman, G.R.1    Nassar, N.2    Cerione, R.A.3
  • 103
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: Central regulatory molecules in Rho GTPase activation
    • DerMardirossian, C. and Bokoch, G. M. (2005) GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol. 15, 356-363
    • (2005) Trends Cell Biol. , vol.15 , pp. 356-363
    • DerMardirossian, C.1    Bokoch, G.M.2
  • 104
    • 26944440432 scopus 로고    scopus 로고
    • RhoGDIs revisited: Novel roles in Rho regulation
    • Dransart, E., Olofsson, B. and Cherfils, J. (2005) RhoGDIs revisited: novel roles in Rho regulation. Traffic 6, 957-966
    • (2005) Traffic , vol.6 , pp. 957-966
    • Dransart, E.1    Olofsson, B.2    Cherfils, J.3
  • 105
    • 0038363325 scopus 로고    scopus 로고
    • Dissociation of GDP dissociation inhibitor and membrane translocation are required for efficient activation of Rac by the Dbl homology-pleckstrin homology region of Tiam
    • Robbe, K., Otto-Bruc, A., Chardin, P. and Antonny, B. (2003) Dissociation of GDP dissociation inhibitor and membrane translocation are required for efficient activation of Rac by the Dbl homology-pleckstrin homology region of Tiam. J. Biol. Chem. 278, 4756-4762
    • (2003) J. Biol. Chem. , vol.278 , pp. 4756-4762
    • Robbe, K.1    Otto-Bruc, A.2    Chardin, P.3    Antonny, B.4
  • 106
  • 108
    • 0031105873 scopus 로고    scopus 로고
    • Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization
    • Colley, W. C., Sung, T. C., Roll, R., Jenco, J., Hammond, S. M., Altshuller, Y., Bar-Sagi, D., Morris, A. J. and Frohman, M. A. (1997) Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization. Curr. Biol. 7, 191-201
    • (1997) Curr. Biol. , vol.7 , pp. 191-201
    • Colley, W.C.1    Sung, T.C.2    Roll, R.3    Jenco, J.4    Hammond, S.M.5    Altshuller, Y.6    Bar-Sagi, D.7    Morris, A.J.8    Frohman, M.A.9
  • 109
    • 0008855384 scopus 로고    scopus 로고
    • Characterization of two alternately spliced forms of phospholipase D1: Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-α
    • Hammond, S. M., Jenco, J. M., Nakashima, S., Cadwallader, K., Gu, Q., Cook, S., Nozawa, Y., Prestwich, G. D., Frohman, M. A. and Morris, A. J. (1997) Characterization of two alternately spliced forms of phospholipase D1: activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-α. J. Biol. Chem. 272, 3860-3868
    • (1997) J. Biol. Chem. , vol.272 , pp. 3860-3868
    • Hammond, S.M.1    Jenco, J.M.2    Nakashima, S.3    Cadwallader, K.4    Gu, Q.5    Cook, S.6    Nozawa, Y.7    Prestwich, G.D.8    Frohman, M.A.9    Morris, A.J.10
  • 110
    • 0033985026 scopus 로고    scopus 로고
    • Phospholipase D regulation and localisation is dependent upon a phosphatidylinositol 4,5-biphosphate-specific PH domain
    • Hodgkin, M. N., Masson, M. R., Powner, D., Saqib, K. M., Porting, C. P. and Wakelam, M. J. (2000) Phospholipase D regulation and localisation is dependent upon a phosphatidylinositol 4,5-biphosphate-specific PH domain. Curr. Biol. 10, 43-46
    • (2000) Curr. Biol. , vol.10 , pp. 43-46
    • Hodgkin, M.N.1    Masson, M.R.2    Powner, D.3    Saqib, K.M.4    Porting, C.P.5    Wakelam, M.J.6
  • 112
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin- and non-clathrin-mediated endocytic regulation of cell signaling
    • Le Roy, C. and Wrana, J. L. (2005) Clathrin- and non-clathrin-mediated endocytic regulation of cell signaling. Nat. Rev. Mol. Cell Biol. 6, 112-126
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2
  • 113
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide connection
    • Liscovitch, M. and Cantley, L. C. (1995) Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell 81, 659-662
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 114
    • 28844478464 scopus 로고    scopus 로고
    • Phosphoinositide regulation of clathrin-mediated endocytosis
    • Haucke, V. (2005) Phosphoinositide regulation of clathrin-mediated endocytosis. Biochem. Soc. Trans. 33, 1285-1289
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1285-1289
    • Haucke, V.1
  • 115
    • 0032546932 scopus 로고    scopus 로고
    • Phosphatidylinositol-4-phosphate 5-kinase localized on the plasma membrane is essential for yeast cell morphogenesis
    • Homma, K., Terui, S., Minemura, M., Qadota, H., Anraku, Y., Kanaho, Y. and Ohya, Y. (1998) Phosphatidylinositol-4-phosphate 5-kinase localized on the plasma membrane is essential for yeast cell morphogenesis. J. Biol. Chem. 273, 15779-15786
    • (1998) J. Biol. Chem. , vol.273 , pp. 15779-15786
    • Homma, K.1    Terui, S.2    Minemura, M.3    Qadota, H.4    Anraku, Y.5    Kanaho, Y.6    Ohya, Y.7
  • 116
    • 0032546798 scopus 로고    scopus 로고
    • MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Desrivieres, S., Cooke, F. T., Parker, P. J. and Hall, M. N. (1998) MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae. J. Biol. Chem. 273, 15787-15793
    • (1998) J. Biol. Chem. , vol.273 , pp. 15787-15793
    • Desrivieres, S.1    Cooke, F.T.2    Parker, P.J.3    Hall, M.N.4
  • 117
    • 24044533530 scopus 로고    scopus 로고
    • Disturbance of sphingolipid biosynthesis abrogates the signaling of Mss4, phosphatidylinositol-4-phosphate 5-kinase, in yeast
    • Kobayashi, T., Takematsu, H., Yamaji, T., Hiramoto, S. and Kozutsumi, Y. (2005) Disturbance of sphingolipid biosynthesis abrogates the signaling of Mss4, phosphatidylinositol-4-phosphate 5-kinase, in yeast. J. Biol. Chem. 280, 18087-18094
    • (2005) J. Biol. Chem. , vol.280 , pp. 18087-18094
    • Kobayashi, T.1    Takematsu, H.2    Yamaji, T.3    Hiramoto, S.4    Kozutsumi, Y.5
  • 118
    • 0034754084 scopus 로고    scopus 로고
    • The PH domain of the yeast GEF Rom2p serves an essential function in vivo
    • Lorberg, A., Jacoby, J. J., Schmitz, H. P. and Heinisch, J. J. (2001) The PH domain of the yeast GEF Rom2p serves an essential function in vivo. Mol. Genet. Genomics 266, 505-513
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 505-513
    • Lorberg, A.1    Jacoby, J.J.2    Schmitz, H.P.3    Heinisch, J.J.4
  • 119
    • 20544432791 scopus 로고    scopus 로고
    • Cell wall integrity signaling in Saccharomyces cerevisiae
    • Levin, D. E. (2005) Cell wall integrity signaling in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 69, 262-291
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 262-291
    • Levin, D.E.1
  • 120
    • 0033637076 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe rho2p GTPase regulates cell wall α-glucan biosynthesis through the protein kinase pck2p
    • Calonge, T. M., Nakano, K., Arellano, M., Arai, R., Katayama, S., Toda, T., Mabuchi, I. and Perez, P. (2000) Schizosaccharomyces pombe rho2p GTPase regulates cell wall α-glucan biosynthesis through the protein kinase pck2p. Mol. Biol. Cell 11, 4393-4401
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4393-4401
    • Calonge, T.M.1    Nakano, K.2    Arellano, M.3    Arai, R.4    Katayama, S.5    Toda, T.6    Mabuchi, I.7    Perez, P.8
  • 121
    • 0030773688 scopus 로고    scopus 로고
    • Localisation of the Schizosaccharomyces pombe rho1p GTPase and its involvement in the organisation of the actin cytoskeleton
    • Arellano, M., Duran, A. and Perez, P. (1997) Localisation of the Schizosaccharomyces pombe rho1p GTPase and its involvement in the organisation of the actin cytoskeleton. J. Cell Sci. 110, 2547-2555
    • (1997) J. Cell Sci. , vol.110 , pp. 2547-2555
    • Arellano, M.1    Duran, A.2    Perez, P.3
  • 122
    • 0034634662 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate 5-kinase Its3 and calcineurin Ppb1 coordinately regulate cytokinesis in fission yeast
    • Zhang, Y., Sugiura, R., Lu, Y., Asami, M., Maeda, T., Itoh, T., Takenawa, T., Shuntoh, H. and Kuno, T. (2000) Phosphatidylinositol 4-phosphate 5-kinase Its3 and calcineurin Ppb1 coordinately regulate cytokinesis in fission yeast. J. Biol. Chem. 275, 35600-35606
    • (2000) J. Biol. Chem. , vol.275 , pp. 35600-35606
    • Zhang, Y.1    Sugiura, R.2    Lu, Y.3    Asami, M.4    Maeda, T.5    Itoh, T.6    Takenawa, T.7    Shuntoh, H.8    Kuno, T.9
  • 123
    • 23044434957 scopus 로고    scopus 로고
    • Phosphatidylinositol-4-phosphate 5-kinase regulates fission yeast cell integrity through a phospholipase C-mediated protein kinase C-independent pathway
    • Deng, L., Sugiura, R., Ohta, K., Tada, K., Suzuki, M., Hirata, M., Nakamura, S., Shuntoh, H. and Kuno, T. (2005) Phosphatidylinositol-4-phosphate 5-kinase regulates fission yeast cell integrity through a phospholipase C-mediated protein kinase C-independent pathway. J. Biol. Chem. 280, 27561-27568
    • (2005) J. Biol. Chem. , vol.280 , pp. 27561-27568
    • Deng, L.1    Sugiura, R.2    Ohta, K.3    Tada, K.4    Suzuki, M.5    Hirata, M.6    Nakamura, S.7    Shuntoh, H.8    Kuno, T.9
  • 124
    • 29244458174 scopus 로고    scopus 로고
    • Rho1-GEFs Rgt1 and Rgf2 are involved in formation of cell wall and septum, while Rgf3 is involved in cytokinesis in fission yeast
    • Mutoh, T., Nakano, K. and Mabuchi, I. (2005) Rho1-GEFs Rgt1 and Rgf2 are involved in formation of cell wall and septum, while Rgf3 is involved in cytokinesis in fission yeast. Genes Cells 10, 1189-1202
    • (2005) Genes Cells , vol.10 , pp. 1189-1202
    • Mutoh, T.1    Nakano, K.2    Mabuchi, I.3
  • 125
    • 33745426423 scopus 로고    scopus 로고
    • Rgf1p is a specific Rho1-GEF that coordinates cell polarization with cell wall biogenesis in fission yeast
    • Garcia, P., Tajadura, V., Garcia, I. and Sanchez, Y. (2006) Rgf1p is a specific Rho1-GEF that coordinates cell polarization with cell wall biogenesis in fission yeast. Mol. Biol. Cell 17, 1620-1631
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1620-1631
    • Garcia, P.1    Tajadura, V.2    Garcia, I.3    Sanchez, Y.4
  • 126
    • 0029024442 scopus 로고
    • Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast
    • Yamamoto, A., DeWald, D. B., Boronenkov, I. V., Anderson, R. A., Emr, S. D. and Koshland, D. (1995) Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast. Mol. Biol. Cell 6, 525-539
    • (1995) Mol. Biol. Cell , vol.6 , pp. 525-539
    • Yamamoto, A.1    DeWald, D.B.2    Boronenkov, I.V.3    Anderson, R.A.4    Emr, S.D.5    Koshland, D.6
  • 127
    • 0032487577 scopus 로고    scopus 로고
    • Fablp is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis
    • Gary, J. D., Wurmser, A. E., Bonangelino, C. J., Weisman, L. S. and Emr, S. D. (1998) Fablp is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis. J. Cell Biol. 143, 65-79
    • (1998) J. Cell Biol. , vol.143 , pp. 65-79
    • Gary, J.D.1    Wurmser, A.E.2    Bonangelino, C.J.3    Weisman, L.S.4    Emr, S.D.5
  • 128
    • 0033607548 scopus 로고    scopus 로고
    • Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases
    • McEwen, R. K., Dove, S. K., Cooke, F. T., Painter, G. F., Holmes, A. B., Shisheva, A., Ohya, Y., Parker, P. J. and Michell, R. H. (1999) Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases. J. Biol. Chem. 274, 33905-33912
    • (1999) J. Biol. Chem. , vol.274 , pp. 33905-33912
    • McEwen, R.K.1    Dove, S.K.2    Cooke, F.T.3    Painter, G.F.4    Holmes, A.B.5    Shisheva, A.6    Ohya, Y.7    Parker, P.J.8    Michell, R.H.9
  • 129
    • 0032488032 scopus 로고    scopus 로고
    • The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae
    • Cooke, F. T., Dove, S. K., McEwen, R. K., Painter, G., Holmes, A. B., Hall, M. N., Michell, R. H. and Parker, P. J. (1998) The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae. Curr. Biol. 8, 1219-1222
    • (1998) Curr. Biol. , vol.8 , pp. 1219-1222
    • Cooke, F.T.1    Dove, S.K.2    McEwen, R.K.3    Painter, G.4    Holmes, A.B.5    Hall, M.N.6    Michell, R.H.7    Parker, P.J.8
  • 130
    • 0037162436 scopus 로고    scopus 로고
    • Phosphoinositide signaling: Vac to the future in fab1 kinase regulation
    • DeWald, D. B. (2002) Phosphoinositide signaling: vac to the future in fab1 kinase regulation. Curr. Biol. 12, R491-492
    • (2002) Curr. Biol. , vol.12
    • DeWald, D.B.1
  • 131
    • 0037128929 scopus 로고    scopus 로고
    • Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p
    • Bonangelino, C. J., Nau, J. J., Duex, J. E., Brinkman, M., Wurmser, A. E., Gary, J. D., Emr, S. D. and Weisman, L. S. (2002) Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p. J. Cell Biol. 156, 1015-1028
    • (2002) J. Cell Biol. , vol.156 , pp. 1015-1028
    • Bonangelino, C.J.1    Nau, J.J.2    Duex, J.E.3    Brinkman, M.4    Wurmser, A.E.5    Gary, J.D.6    Emr, S.D.7    Weisman, L.S.8
  • 132
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • Odorizzi, G., Babst, M. and Emr, S. D. (1998) Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell 95, 847-858
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 134
    • 30944461203 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate: Metabolism and cellular functions
    • Michell, R. H., Heath, V. L., Lemmon, M. A. and Dove, S. K. (2006) Phosphatidylinositol 3,5-bisphosphate: metabolism and cellular functions. Trends Biochem. Sci. 31, 52-63
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 52-63
    • Michell, R.H.1    Heath, V.L.2    Lemmon, M.A.3    Dove, S.K.4
  • 135
    • 33645558443 scopus 로고    scopus 로고
    • Weak acid and alkali stress regulate phosphatidylinositol bisphosphate synthesis in Saccharomyces cerevisiae
    • Mollapour, M., Phelan, J. P., Millson, S. H., Piper, P. W. and Cooke, F. T. (2006) Weak acid and alkali stress regulate phosphatidylinositol bisphosphate synthesis in Saccharomyces cerevisiae. Biochem. J. 395, 73-80
    • (2006) Biochem. J. , vol.395 , pp. 73-80
    • Mollapour, M.1    Phelan, J.P.2    Millson, S.H.3    Piper, P.W.4    Cooke, F.T.5
  • 137
    • 0037040875 scopus 로고    scopus 로고
    • Anionic phospholipids regulate native and expressed epithelial sodium channel (ENaC)
    • Ma, H. P., Saxena, S. and Warnock, D. G. (2002) Anionic phospholipids regulate native and expressed epithelial sodium channel (ENaC). J. Biol. Chem. 277, 7641-7644
    • (2002) J. Biol. Chem. , vol.277 , pp. 7641-7644
    • Ma, H.P.1    Saxena, S.2    Warnock, D.G.3
  • 138
    • 0037023759 scopus 로고    scopus 로고
    • 2) stimulates epithelial sodium channel activity in A6 cells
    • 2) stimulates epithelial sodium channel activity in A6 cells. J. Biol. Chem. 277, 11965-11969
    • (2002) J. Biol. Chem. , vol.277 , pp. 11965-11969
    • Yue, G.1    Malik, B.2    Yue, G.3    Eaton, D.C.4
  • 144
    • 27744586089 scopus 로고    scopus 로고
    • Direct modulation of Kir channel gating by membrane phosphatidylinositol 4,5-bisphosphate
    • Enkvetchakul, D., Jeliazkova, I. and Nichols, C. G. (2005) Direct modulation of Kir channel gating by membrane phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 280, 35785-35788
    • (2005) J. Biol. Chem. , vol.280 , pp. 35785-35788
    • Enkvetchakul, D.1    Jeliazkova, I.2    Nichols, C.G.3
  • 146
    • 4444359501 scopus 로고    scopus 로고
    • Characteristic interactions with phosphatidylinositol 4,5-bisphosphate determine regulation of Kir channels by diverse modulators
    • Du, X., Zhang, H., Lopes, C., Mirshahi, T., Rohacs, T. and Logothetis, D. E. (2004) Characteristic interactions with phosphatidylinositol 4,5-bisphosphate determine regulation of Kir channels by diverse modulators. J. Biol. Chem. 279, 37271-37281
    • (2004) J. Biol. Chem. , vol.279 , pp. 37271-37281
    • Du, X.1    Zhang, H.2    Lopes, C.3    Mirshahi, T.4    Rohacs, T.5    Logothetis, D.E.6
  • 147
    • 0141794172 scopus 로고    scopus 로고
    • Role of the small GTPase Rho in modulation of the inwardly rectifying potassium channel Kir2.1
    • 146a Jones, S. V. P. (2003) Role of the small GTPase Rho in modulation of the inwardly rectifying potassium channel Kir2.1. Mol. Pharmacol. 64, 987-993
    • (2003) Mol. Pharmacol. , vol.64 , pp. 987-993
    • Jones, S.V.P.1
  • 148
    • 0035003359 scopus 로고    scopus 로고
    • Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel
    • Tong, Y., Brandt, G. S., Li, M., Shapovalov, G., Slimko, E., Karschin, A., Dougherty, D. A. and Lester, H. A. (2001) Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel. J. Gen. Physiol. 117, 103-118
    • (2001) J. Gen. Physiol. , vol.117 , pp. 103-118
    • Tong, Y.1    Brandt, G.S.2    Li, M.3    Shapovalov, G.4    Slimko, E.5    Karschin, A.6    Dougherty, D.A.7    Lester, H.A.8
  • 150
    • 0032511197 scopus 로고    scopus 로고
    • The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel
    • Cachera, T. G., Morielli, A. D. and Peralta, E. G. (1998) The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel. Cell 93, 1077-1085
    • (1998) Cell , vol.93 , pp. 1077-1085
    • Cachera, T.G.1    Morielli, A.D.2    Peralta, E.G.3
  • 154
    • 28244499948 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate rescues TRPM4 channels from desensitization
    • Zhang, Z., Okawa, H., Wang, Y. and Liman, E. R. (2005) Phosphatidylinositol 4,5-bisphosphate rescues TRPM4 channels from desensitization. J. Biol. Chem. 280, 39185-39192
    • (2005) J. Biol. Chem. , vol.280 , pp. 39185-39192
    • Zhang, Z.1    Okawa, H.2    Wang, Y.3    Liman, E.R.4
  • 155
    • 0344149569 scopus 로고    scopus 로고
    • 2 regulate the taste transduction ion channel TRPM5
    • 2 regulate the taste transduction ion channel TRPM5. Proc. Natl. Acad. Sci. U.S.A. 100, 15160-15165
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 15160-15165
    • Liu, D.1    Liman, E.R.2
  • 156
    • 18644381102 scopus 로고    scopus 로고
    • Functional recovery from desensitization of vanilloid receptor TRPV1 requires resynthesis of phosphatidylinositol 4,5-bisphosphate
    • Liu, B., Zhang, C. and Qin, F. (2005) Functional recovery from desensitization of vanilloid receptor TRPV1 requires resynthesis of phosphatidylinositol 4,5-bisphosphate. J. Neurosci. 25, 4835-4843
    • (2005) J. Neurosci. , vol.25 , pp. 4835-4843
    • Liu, B.1    Zhang, C.2    Qin, F.3
  • 158
    • 24344482068 scopus 로고    scopus 로고
    • PKD2 functions as an epidermal growth factor-activated plasma membrane channel
    • Ma, R., Li, W. P., Rundle, D., Kong, J., Akbarali, H. I. and Tsiokas, L. (2005) PKD2 functions as an epidermal growth factor-activated plasma membrane channel. Mol. Cell. Biol. 25, 8285-8298
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8285-8298
    • Ma, R.1    Li, W.P.2    Rundle, D.3    Kong, J.4    Akbarali, H.I.5    Tsiokas, L.6


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