메뉴 건너뛰기




Volumn 31, Issue 6, 2011, Pages 1240-1251

Membrane environment exerts an important influence on Rac-mediated activation of phospholipase Cγ2

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOLIPASE C GAMMA2; RAC2 PROTEIN;

EID: 79952256065     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01408-10     Document Type: Article
Times cited : (25)

References (43)
  • 2
    • 58149355793 scopus 로고    scopus 로고
    • Structural changes of yellow Cameleon domains observed by quantitative FRET analysis and polarized fluorescence correlation spectroscopy
    • Borst, J. W., et al. 2008. Structural changes of yellow Cameleon domains observed by quantitative FRET analysis and polarized fluorescence correlation spectroscopy. Biophys. J. 95:5399-5411.
    • (2008) Biophys. J. , vol.95 , pp. 5399-5411
    • Borst, J.W.1
  • 3
    • 79551613763 scopus 로고    scopus 로고
    • PLC regulation: Emerging pictures for molecular mechanisms
    • 24 September [Epub ahead of print.] doi:10.1016/j.tibs.2010.08.003
    • Bunney, T. D., and M. Katan. 24 September 2010. PLC regulation: emerging pictures for molecular mechanisms. Trends Biochem. Sci. [Epub ahead of print.] doi:10.1016/j.tibs.2010.08.003.
    • (2010) Trends Biochem. Sci.
    • Bunney, T.D.1    Katan, M.2
  • 4
    • 64749102105 scopus 로고    scopus 로고
    • Structural insights into formation of an active signaling complex between Rac and phospholipase C gamma 2
    • Bunney, T. D., et al. 2009. Structural insights into formation of an active signaling complex between Rac and phospholipase C gamma 2. Mol. Cell 34:223-233.
    • (2009) Mol. Cell , vol.34 , pp. 223-233
    • Bunney, T.D.1
  • 5
    • 0033604513 scopus 로고    scopus 로고
    • Phospholipase C-gamma as a signal-transducing element
    • Carpenter, G., and Q. Ji. 1999. Phospholipase C-gamma as a signal-transducing element. Exp. Cell Res. 253:15-24.
    • (1999) Exp. Cell Res. , vol.253 , pp. 15-24
    • Carpenter, G.1    Ji, Q.2
  • 6
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole, C., J. D. Barber, and G. J. Barton. 2008. The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 36:W197-W201.
    • (2008) Nucleic Acids Res. , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 7
    • 77749246288 scopus 로고    scopus 로고
    • Phospholipase C gamma 2 is critical for development of a murine model of inflammatory arthritis by affecting actin dynamics in dendritic cells
    • Cremasco, V., et al. 2010. Phospholipase C gamma 2 is critical for development of a murine model of inflammatory arthritis by affecting actin dynamics in dendritic cells. PLoS One 5:e8909.
    • (2010) PLoS One , vol.5
    • Cremasco, V.1
  • 8
    • 33846605114 scopus 로고    scopus 로고
    • Intramolecular regulation of phospholipase C-gamma1 by its C-terminal Src homology 2 domain
    • DeBell, K., et al. 2007. Intramolecular regulation of phospholipase C-gamma1 by its C-terminal Src homology 2 domain. Mol. Cell. Biol. 27:854-863.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 854-863
    • DeBell, K.1
  • 9
    • 0032496273 scopus 로고    scopus 로고
    • Catalytic domain of phosphoinositide-specific phospholipase C (PLC). Mutational analysis of residues within the active site and hydrophobic ridge of plcdelta1
    • Ellis, M. V., et al. 1998. Catalytic domain of phosphoinositide-specific phospholipase C (PLC). Mutational analysis of residues within the active site and hydrophobic ridge of plcdelta1. J. Biol. Chem. 273:11650-11659.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11650-11659
    • Ellis, M.V.1
  • 10
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen, L. O., O. Perisic, R. Cheung, M. Katan, and R. L. Williams. 1996. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature 380:595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 11
    • 69249083630 scopus 로고    scopus 로고
    • Characterization of phospholipase C gamma enzymes with gain-of-function mutations
    • Everett, K. L., et al. 2009. Characterization of phospholipase C gamma enzymes with gain-of-function mutations. J. Biol. Chem. 284:23083-23093.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23083-23093
    • Everett, K.L.1
  • 12
    • 78149268559 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-induced activation of phospholipase C-{gamma} isozymes
    • Gresset, A., S. N. Hicks, T. K. Harden, and J. Sondek. 2010. Mechanism of phosphorylation-induced activation of phospholipase C-{gamma} isozymes. J. Biol. Chem. 285:35836-35847.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35836-35847
    • Gresset, A.1    Hicks, S.N.2    Harden, T.K.3    Sondek, J.4
  • 13
    • 77953293697 scopus 로고    scopus 로고
    • Molecular mechanisms in signal transduction at the membrane
    • Groves, J. T., and J. Kuriyan. 2010. Molecular mechanisms in signal transduction at the membrane. Nat. Struct. Mol. Biol. 17:659-665.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 659-665
    • Groves, J.T.1    Kuriyan, J.2
  • 14
    • 67649470550 scopus 로고    scopus 로고
    • Integrin alpha2beta1 induces phosphorylation-dependent and phosphorylation-independent activation of phospholipase Cgamma2 in platelets: Role of Src kinase and Rac GTPase
    • Guidetti, G. F., et al. 2009. Integrin alpha2beta1 induces phosphorylation-dependent and phosphorylation-independent activation of phospholipase Cgamma2 in platelets: role of Src kinase and Rac GTPase. J. Thromb. Haemost. 7:1200-1206.
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 1200-1206
    • Guidetti, G.F.1
  • 15
    • 77950473766 scopus 로고    scopus 로고
    • Differential regulation of phospholipase C-beta2 activity and membrane interaction by Galphaq, Gbeta1gamma2, and Rac2
    • Gutman, O., C. Walliser, T. Piechulek, P. Gierschik, and Y. I. Henis. 2010. Differential regulation of phospholipase C-beta2 activity and membrane interaction by Galphaq, Gbeta1gamma2, and Rac2. J. Biol. Chem. 285:3905-3915.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3905-3915
    • Gutman, O.1    Walliser, C.2    Piechulek, T.3    Gierschik, P.4    Henis, Y.I.5
  • 16
    • 66349113776 scopus 로고    scopus 로고
    • Phospholipase C isozymes as effectors of Ras superfamily GTPases
    • Harden, T. K., S. N. Hicks, and J. Sondek. 2009. Phospholipase C isozymes as effectors of Ras superfamily GTPases. J. Lipid Res. 50(Suppl.):S243-S248.
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Harden, T.K.1    Hicks, S.N.2    Sondek, J.3
  • 17
    • 48349120928 scopus 로고    scopus 로고
    • General and versatile autoinhibition of PLC isozymes
    • Hicks, S. N., et al. 2008. General and versatile autoinhibition of PLC isozymes. Mol. Cell 31:383-394.
    • (2008) Mol. Cell , vol.31 , pp. 383-394
    • Hicks, S.N.1
  • 18
    • 0030666620 scopus 로고    scopus 로고
    • Inhibition of phosphoinositide hydrolysis and cell growth of Swiss 3T3 cells by myristoylated phospholipase C inhibitor peptides
    • Homma, M. K., M. Yamasaki, S. Ohmi, and Y. Homma. 1997. Inhibition of phosphoinositide hydrolysis and cell growth of Swiss 3T3 cells by myristoylated phospholipase C inhibitor peptides. J. Biochem. 122:738-742. (Pubitemid 27474942)
    • (1997) Journal of Biochemistry , vol.122 , Issue.4 , pp. 738-742
    • Komma, M.K.1    Yamasaki, M.2    Ohmi, S.3    Homma, Y.4
  • 19
    • 0026801534 scopus 로고
    • Inhibitory effect of src homology (SH) 2/SH3 fragments of phospholipase C-gamma on the catalytic activity of phospholipase C isoforms. Identification of a novel phospholipase C inhibitor region
    • Homma, Y., and T. Takenawa. 1992. Inhibitory effect of src homology (SH) 2/SH3 fragments of phospholipase C-gamma on the catalytic activity of phospholipase C isoforms. Identification of a novel phospholipase C inhibitor region. J. Biol. Chem. 267:21844-21849.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21844-21849
    • Homma, Y.1    Takenawa, T.2
  • 20
    • 0029820560 scopus 로고    scopus 로고
    • Enhanced phospholipase C-gamma1 activity produced by association of independently expressed X and Y domain polypeptides
    • Horstman, D. A., K. DeStefano, and G. Carpenter. 1996. Enhanced phospholipase C-gamma1 activity produced by association of independently expressed X and Y domain polypeptides. Proc. Natl. Acad. Sci. U. S. A. 93:7518-7521.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7518-7521
    • Horstman, D.A.1    DeStefano, K.2    Carpenter, G.3
  • 21
    • 33845367647 scopus 로고    scopus 로고
    • Crystal structure of Rac1 bound to its effector phospholipase C-beta2
    • Jezyk, M. R., et al. 2006. Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat. Struct. Mol. Biol. 13:1135-1140.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1135-1140
    • Jezyk, M.R.1
  • 22
    • 33644840483 scopus 로고    scopus 로고
    • New insights into the families of PLC enzymes: Looking back and going forward
    • Katan, M. 2005. New insights into the families of PLC enzymes: looking back and going forward. Biochem. J. 391:e7-e9.
    • (2005) Biochem. J. , vol.391
    • Katan, M.1
  • 25
    • 65449163397 scopus 로고    scopus 로고
    • A compact, multidimensional spectrofluorometer exploiting supercontinuum generation
    • Manning, H. B., et al. 2008. A compact, multidimensional spectrofluorometer exploiting supercontinuum generation. J. Biophotonics 1:494-505.
    • (2008) J. Biophotonics , vol.1 , pp. 494-505
    • Manning, H.B.1
  • 28
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips, R., T. Ursell, P. Wiggins, and P. Sens. 2009. Emerging roles for lipids in shaping membrane-protein function. Nature 459:379-385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 29
    • 28244479373 scopus 로고    scopus 로고
    • Isozyme-specific stimulation of phospholipase C-gamma2 by Rac GTPases
    • Piechulek, T., et al. 2005. Isozyme-specific stimulation of phospholipase C-gamma2 by Rac GTPases. J. Biol. Chem. 280:38923-38931.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38923-38931
    • Piechulek, T.1
  • 30
    • 59849108084 scopus 로고    scopus 로고
    • Rac1 is essential for phospholipase C-gamma2 activation in platelets
    • Pleines, I., et al. 2009. Rac1 is essential for phospholipase C-gamma2 activation in platelets. Pflugers Arch. 457:1173-1185.
    • (2009) Pflugers Arch. , vol.457 , pp. 1173-1185
    • Pleines, I.1
  • 31
    • 15444377640 scopus 로고    scopus 로고
    • Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-gamma1
    • Poulin, B., F. Sekiya, and S. G. Rhee. 2005. Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-gamma1. Proc. Natl. Acad. Sci. U. S. A. 102:4276-4281.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4276-4281
    • Poulin, B.1    Sekiya, F.2    Rhee, S.G.3
  • 32
    • 0035930574 scopus 로고    scopus 로고
    • Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling
    • Rodriguez, R., et al. 2001. Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling. J. Biol. Chem. 276:47982-47992.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47982-47992
    • Rodriguez, R.1
  • 33
    • 65549091909 scopus 로고    scopus 로고
    • Practical and reliable FRET/FLIM pair of fluorescent proteins
    • Shcherbo, D., et al. 2009. Practical and reliable FRET/FLIM pair of fluorescent proteins. BMC Biotechnol. 9:24.
    • (2009) BMC Biotechnol. , vol.9 , pp. 24
    • Shcherbo, D.1
  • 34
    • 12444279041 scopus 로고    scopus 로고
    • Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants
    • DOI 10.1038/sj.onc.1208168
    • Sorli, S. C., T. D. Bunney, P. H. Sugden, H. F. Paterson, and M. Katan. 2005. Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants. Oncogene 24:90-100. (Pubitemid 40143868)
    • (2005) Oncogene , vol.24 , Issue.1 , pp. 90-100
    • Sorli, S.C.1    Bunney, T.D.2    Sugden, P.H.3    Paterson, H.F.4    Katan, M.5
  • 35
    • 0035901553 scopus 로고    scopus 로고
    • 2
    • DOI 10.1021/bi0020325
    • Stahelin, R. V., and W. Cho. 2001. Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: a surface plasmon resonance study on phospholipases A2. Biochemistry 40:4672-4678. (Pubitemid 32374655)
    • (2001) Biochemistry , vol.40 , Issue.15 , pp. 4672-4678
    • Stahelin, R.V.1    Cho, W.2
  • 36
    • 46249091922 scopus 로고    scopus 로고
    • Multiple roles of phosphoinositide-specific phospholipase C isozymes
    • Suh, P. G., et al. 2008. Multiple roles of phosphoinositide-specific phospholipase C isozymes. BMB Rep. 41:415-434.
    • (2008) BMB Rep. , vol.41 , pp. 415-434
    • Suh, P.G.1
  • 37
    • 0025978171 scopus 로고
    • Platelet-derived growth factor increases the in vivo activity of phospholipase C-gamma 1 and phospholipase C-gamma 2
    • Sultzman, L., C. Ellis, L. L. Lin, T. Pawson, and J. Knopf. 1991. Platelet-derived growth factor increases the in vivo activity of phospholipase C-gamma 1 and phospholipase C-gamma 2. Mol. Cell. Biol. 11:2018-2025.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2018-2025
    • Sultzman, L.1    Ellis, C.2    Lin, L.L.3    Pawson, T.4    Knopf, J.5
  • 38
    • 73649144225 scopus 로고    scopus 로고
    • Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs
    • Visser, A. J., et al. 2010. Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs. Eur. Biophys. J. 39:241-253.
    • (2010) Eur. Biophys. J. , vol.39 , pp. 241-253
    • Visser, A.J.1
  • 39
    • 0034053143 scopus 로고    scopus 로고
    • One- and two-photon excited fluorescence lifetimes and anisotropy decays of green fluorescent proteins
    • Volkmer, A., V. Subramaniam, D. J. Birch, and T. M. Jovin. 2000. One- and two-photon excited fluorescence lifetimes and anisotropy decays of green fluorescent proteins. Biophys. J. 78:1589-1598.
    • (2000) Biophys. J. , vol.78 , pp. 1589-1598
    • Volkmer, A.1    Subramaniam, V.2    Birch, D.J.3    Jovin, T.M.4
  • 40
    • 57649210150 scopus 로고    scopus 로고
    • Rac regulates its effector phospholipase Cgamma2 through interaction with a split pleckstrin homology domain
    • Walliser, C., et al. 2008. rac regulates its effector phospholipase Cgamma2 through interaction with a split pleckstrin homology domain. J. Biol. Chem. 283:30351-30362.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30351-30362
    • Walliser, C.1
  • 41
    • 66149096239 scopus 로고    scopus 로고
    • Fluorescence fluctuation spectroscopy of mCherry in living cells
    • Wu, B., Y. Chen, and J. D. Muller. 2009. Fluorescence fluctuation spectroscopy of mCherry in living cells. Biophys. J. 96:2391-2404.
    • (2009) Biophys. J. , vol.96 , pp. 2391-2404
    • Wu, B.1    Chen, Y.2    Muller, J.D.3
  • 42
    • 51849128358 scopus 로고    scopus 로고
    • Class I PI3K in oncogenic cellular transformation
    • Zhao, L., and P. K. Vogt. 2008. Class I PI3K in oncogenic cellular transformation. Oncogene 27:5486-5496.
    • (2008) Oncogene , vol.27 , pp. 5486-5496
    • Zhao, L.1    Vogt, P.K.2
  • 43
    • 40649096375 scopus 로고    scopus 로고
    • Helical domain and kinase domain mutations in p110alpha of phosphatidylinositol 3-kinase induce gain of function by different mechanisms
    • Zhao, L., and P. K. Vogt. 2008. Helical domain and kinase domain mutations in p110alpha of phosphatidylinositol 3-kinase induce gain of function by different mechanisms. Proc. Natl. Acad. Sci. U. S. A. 105:2652-2657.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 2652-2657
    • Zhao, L.1    Vogt, P.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.