메뉴 건너뛰기




Volumn 73, Issue 2, 2007, Pages 270-278

Calmodulin potentiates Gβγ activation of phospholipase C-β3

Author keywords

1321N1 cells; Calmodulin; Fluorescence anisotropy; Gbetagamma; Phosphatidylinositol hydrolysis; Phospholipase C beta

Indexed keywords

CALCIUM; CALMODULIN; CALMODULIN INHIBITOR; CARBACHOL; DIMER; FLUPHENAZINE; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; ISOENZYME; MUSCARINIC RECEPTOR; N (4 AMINOBUTYL) 5 CHLORO 2 NAPSYLAMIDE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PHOSPHOLIPASE C BETA1; PHOSPHOLIPASE C BETA3; TRITIUM;

EID: 33845213288     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.10.004     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 0141594888 scopus 로고    scopus 로고
    • Calmodulin is a phospholipase C-{beta} interacting protein
    • McCullar J.S., Larsen S.A., Millimaki R.A., and Filtz T.M. Calmodulin is a phospholipase C-{beta} interacting protein. J Biol Chem 278 36 (2003) 33708-33713
    • (2003) J Biol Chem , vol.278 , Issue.36 , pp. 33708-33713
    • McCullar, J.S.1    Larsen, S.A.2    Millimaki, R.A.3    Filtz, T.M.4
  • 2
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi M.J., and Pentyala S.N. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol Rev 80 (2000) 1291-1335
    • (2000) Physiol Rev , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 3
    • 22144495354 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel phospholipase C, PLC-eta
    • Hwang J.I., Oh Y.S., Shin K.J., Kim H., Ryu S.H., and Suh P.G. Molecular cloning and characterization of a novel phospholipase C, PLC-eta. Biochem J 389 Pt 1 (2005) 181-186
    • (2005) Biochem J , vol.389 , Issue.PART 1 , pp. 181-186
    • Hwang, J.I.1    Oh, Y.S.2    Shin, K.J.3    Kim, H.4    Ryu, S.H.5    Suh, P.G.6
  • 4
    • 0035951771 scopus 로고    scopus 로고
    • Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras
    • Song C., Hu C.-D., Masago M., Kariya K.-I., Yamawaki-Kataoka Y., Shibatohge M., et al. Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J Biol Chem 276 4 (2001) 2752-2757
    • (2001) J Biol Chem , vol.276 , Issue.4 , pp. 2752-2757
    • Song, C.1    Hu, C.-D.2    Masago, M.3    Kariya, K.-I.4    Yamawaki-Kataoka, Y.5    Shibatohge, M.6
  • 6
    • 0027120839 scopus 로고
    • Members of the Gq alpha subunit gene family activate phospholipase C beta isozymes
    • Lee C.H., Park D., Wu D., Rhee S.G., and Simon M.I. Members of the Gq alpha subunit gene family activate phospholipase C beta isozymes. J Biol Chem 267 23 (1992) 16044-16047
    • (1992) J Biol Chem , vol.267 , Issue.23 , pp. 16044-16047
    • Lee, C.H.1    Park, D.2    Wu, D.3    Rhee, S.G.4    Simon, M.I.5
  • 7
    • 0029670037 scopus 로고    scopus 로고
    • Identification of determinants in the alpha-subunit of Gq required for phospholipase C activation
    • Venkatakrishnan G., and Exton J.H. Identification of determinants in the alpha-subunit of Gq required for phospholipase C activation. J Biol Chem 271 9 (1996) 5066-5072
    • (1996) J Biol Chem , vol.271 , Issue.9 , pp. 5066-5072
    • Venkatakrishnan, G.1    Exton, J.H.2
  • 8
    • 0026500077 scopus 로고
    • Activation of phospholipase C by the alpha subunits of the Gq and G11 proteins in transfected Cos-7 cells
    • Wu D.Q., Lee C.H., Rhee S.G., and Simon M.I. Activation of phospholipase C by the alpha subunits of the Gq and G11 proteins in transfected Cos-7 cells. J Biol Chem 267 3 (1992) 1811-1817
    • (1992) J Biol Chem , vol.267 , Issue.3 , pp. 1811-1817
    • Wu, D.Q.1    Lee, C.H.2    Rhee, S.G.3    Simon, M.I.4
  • 9
    • 0027418803 scopus 로고
    • Activation of phospholipase C isozymes by G protein βγ subunits
    • Park D., Jhon D.-Y., Lee C.-W., Lee K.-H., and Rhee S.G. Activation of phospholipase C isozymes by G protein βγ subunits. J Biol Chem 268 (1993) 4573-4576
    • (1993) J Biol Chem , vol.268 , pp. 4573-4576
    • Park, D.1    Jhon, D.-Y.2    Lee, C.-W.3    Lee, K.-H.4    Rhee, S.G.5
  • 10
    • 0030995012 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C isozymes
    • Rhee S.G., and Bae Y.S. Regulation of phosphoinositide-specific phospholipase C isozymes. J Biol Chem 272 24 (1997) 15045-15048
    • (1997) J Biol Chem , vol.272 , Issue.24 , pp. 15045-15048
    • Rhee, S.G.1    Bae, Y.S.2
  • 11
    • 22044443427 scopus 로고    scopus 로고
    • The relative role of PLC{beta} and PI3K{gamma} in platelet activation
    • Lian L., Wang Y., Draznin J., Eslin D., Bennett J.S., Poncz M., et al. The relative role of PLC{beta} and PI3K{gamma} in platelet activation. Blood 106 1 (2005) 110-117
    • (2005) Blood , vol.106 , Issue.1 , pp. 110-117
    • Lian, L.1    Wang, Y.2    Draznin, J.3    Eslin, D.4    Bennett, J.S.5    Poncz, M.6
  • 12
    • 13044277562 scopus 로고    scopus 로고
    • Genetic alteration of phospholipase C beta 3 expression modulates behavioral and cellular responses to {micro} opioids
    • Xie W., Samoriski G.M., McLaughlin J.P., Romoser V.A., Smrcka A., Hinkle P.M., et al. Genetic alteration of phospholipase C beta 3 expression modulates behavioral and cellular responses to {micro} opioids. PNAS 96 18 (1999) 10385-10390
    • (1999) PNAS , vol.96 , Issue.18 , pp. 10385-10390
    • Xie, W.1    Samoriski, G.M.2    McLaughlin, J.P.3    Romoser, V.A.4    Smrcka, A.5    Hinkle, P.M.6
  • 13
    • 0031876257 scopus 로고    scopus 로고
    • Phospholipase C (EC 3.1.4. 11): a malignancy linked signal transduction enzyme
    • Yang H., Shen F., Herenyiova M., and Weber G. Phospholipase C (EC 3.1.4. 11): a malignancy linked signal transduction enzyme. Anticancer Res 18 3A (1998) 1399-1404
    • (1998) Anticancer Res , vol.18 , Issue.3 A , pp. 1399-1404
    • Yang, H.1    Shen, F.2    Herenyiova, M.3    Weber, G.4
  • 14
    • 0032541171 scopus 로고    scopus 로고
    • Phosphorylation of serine 1105 by protein kinase A inhibits phospholipase Cbeta3 stimulation by Galphaq
    • Yue C., Dodge K.L., Weber G., and Sanborn B.M. Phosphorylation of serine 1105 by protein kinase A inhibits phospholipase Cbeta3 stimulation by Galphaq. J Biol Chem 273 29 (1998) 18023-18027
    • (1998) J Biol Chem , vol.273 , Issue.29 , pp. 18023-18027
    • Yue, C.1    Dodge, K.L.2    Weber, G.3    Sanborn, B.M.4
  • 15
    • 0032918096 scopus 로고    scopus 로고
    • Suppression of the neoplastic phenotype by transfection of phospholipase C beta 3 to neuroendocrine tumor cells
    • Stålberg P., Wang S., Larsson C., Weber G., Öberg K., Gobl A., et al. Suppression of the neoplastic phenotype by transfection of phospholipase C beta 3 to neuroendocrine tumor cells. FEBS Lett 450 3 (1999) 210-216
    • (1999) FEBS Lett , vol.450 , Issue.3 , pp. 210-216
    • Stålberg, P.1    Wang, S.2    Larsson, C.3    Weber, G.4    Öberg, K.5    Gobl, A.6
  • 16
    • 0028170327 scopus 로고
    • The phospholipase C beta 3 gene located in the MEN1 region shows loss of expression in endocrine tumours
    • Weber G., Friedman E., Grimmond S., Hayward N., Phelan C., Skogseid B., et al. The phospholipase C beta 3 gene located in the MEN1 region shows loss of expression in endocrine tumours. Hum Mol Genet 3 10 (1994) 1775-1781
    • (1994) Hum Mol Genet , vol.3 , Issue.10 , pp. 1775-1781
    • Weber, G.1    Friedman, E.2    Grimmond, S.3    Hayward, N.4    Phelan, C.5    Skogseid, B.6
  • 17
    • 0032415362 scopus 로고    scopus 로고
    • Targeted disruption of the mouse phospholipase C beta 3 gene results in early embryonic lethality
    • Wang S., Gebre-Medhin S., Betsholtz C., Stalberg P., Zhou Y., Larsson C., et al. Targeted disruption of the mouse phospholipase C beta 3 gene results in early embryonic lethality. FEBS Lett 441 (1998) 261-265
    • (1998) FEBS Lett , vol.441 , pp. 261-265
    • Wang, S.1    Gebre-Medhin, S.2    Betsholtz, C.3    Stalberg, P.4    Zhou, Y.5    Larsson, C.6
  • 18
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: a prototypical calcium sensor
    • Chin D., and Means A.R. Calmodulin: a prototypical calcium sensor. Trends Cell Biol 10 8 (2000) 322-328
    • (2000) Trends Cell Biol , vol.10 , Issue.8 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 19
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • Vetter S.W., and Leclerc E. Novel aspects of calmodulin target recognition and activation. Eur J Biochem 270 3 (2003) 404-414
    • (2003) Eur J Biochem , vol.270 , Issue.3 , pp. 404-414
    • Vetter, S.W.1    Leclerc, E.2
  • 21
    • 0029919963 scopus 로고    scopus 로고
    • Dityrosine formation in calmodulin: cross-linking and polymerization catalyzed by arthromyces peroxidase
    • Malencik D.A., and Anderson S.R. Dityrosine formation in calmodulin: cross-linking and polymerization catalyzed by arthromyces peroxidase. Biochemistry 35 14 (1996) 4375-4386
    • (1996) Biochemistry , vol.35 , Issue.14 , pp. 4375-4386
    • Malencik, D.A.1    Anderson, S.R.2
  • 22
    • 0029856722 scopus 로고    scopus 로고
    • Purification G protein subunit regulation of phospholipase C-β from Xenopus laevis oocytes
    • Filtz T.M., Paterson A., and Harden T.K. Purification G protein subunit regulation of phospholipase C-β from Xenopus laevis oocytes. J Biol Chem 271 (1996) 31121-31126
    • (1996) J Biol Chem , vol.271 , pp. 31121-31126
    • Filtz, T.M.1    Paterson, A.2    Harden, T.K.3
  • 23
    • 0036143898 scopus 로고    scopus 로고
    • A unique fold of phospholipase C-mediates dimerization and interaction with Gq
    • Singer A.U., Waldo G.L., Harden T.K., and Sondek J. A unique fold of phospholipase C-mediates dimerization and interaction with Gq. Nat Struct Biol 9 (2002) 32-36
    • (2002) Nat Struct Biol , vol.9 , pp. 32-36
    • Singer, A.U.1    Waldo, G.L.2    Harden, T.K.3    Sondek, J.4
  • 24
    • 1642513141 scopus 로고    scopus 로고
    • Expression, purification and reconstitution of recombinant phospholipase C-β isoenzymes
    • Paterson A., and Harden T.K. Expression, purification and reconstitution of recombinant phospholipase C-β isoenzymes. Meth Neurosci 29 (1996) 246-263
    • (1996) Meth Neurosci , vol.29 , pp. 246-263
    • Paterson, A.1    Harden, T.K.2
  • 27
    • 30944438497 scopus 로고    scopus 로고
    • Nongenomic action of progesterone inhibits oxytocin-induced phosphoinositide hydrolysis and prostaglandin F2{alpha} secretion in the ovine endometrium
    • Bishop C.V., and Stormshak F. Nongenomic action of progesterone inhibits oxytocin-induced phosphoinositide hydrolysis and prostaglandin F2{alpha} secretion in the ovine endometrium. Endocrinology 147 2 (2006) 937-942
    • (2006) Endocrinology , vol.147 , Issue.2 , pp. 937-942
    • Bishop, C.V.1    Stormshak, F.2
  • 28
    • 0033514304 scopus 로고    scopus 로고
    • Determination of the affinities between heterotrimeric G protein subunits and their phospholipase C-beta effectors
    • Runnels L.W., and Scarlata S.F. Determination of the affinities between heterotrimeric G protein subunits and their phospholipase C-beta effectors. J Biochem 38 (1999) 1488-1496
    • (1999) J Biochem , vol.38 , pp. 1488-1496
    • Runnels, L.W.1    Scarlata, S.F.2
  • 29
    • 0034705237 scopus 로고    scopus 로고
    • 2+/calmodulin reverses phosphatidylinositol 3,4,5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity
    • 2+/calmodulin reverses phosphatidylinositol 3,4,5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity. J Biol Chem 275 25 (2000) 18962-24300
    • (2000) J Biol Chem , vol.275 , Issue.25 , pp. 18962-24300
    • Popov, S.G.1    Krishna, U.M.2    Falck, J.R.3    Wilkie, T.M.4
  • 30
    • 0035895882 scopus 로고    scopus 로고
    • The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate
    • Wang J., Arbuzova A., Hangyas-Mihalyne G., and McLaughlin S. The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. J Biol Chem 276 7 (2001) 5012-5019
    • (2001) J Biol Chem , vol.276 , Issue.7 , pp. 5012-5019
    • Wang, J.1    Arbuzova, A.2    Hangyas-Mihalyne, G.3    McLaughlin, S.4
  • 31
    • 0036138931 scopus 로고    scopus 로고
    • Calmodulin is a limiting factor in the cell
    • Persechini A., and Stemmer P.M. Calmodulin is a limiting factor in the cell. Trends Cardiovasc Med 12 1 (2002) 32-37
    • (2002) Trends Cardiovasc Med , vol.12 , Issue.1 , pp. 32-37
    • Persechini, A.1    Stemmer, P.M.2
  • 33
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads A.R., and Friedberg F. Sequence motifs for calmodulin recognition. FASEB J 11 5 (1997) 331-340
    • (1997) FASEB J , vol.11 , Issue.5 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 35
    • 0034700978 scopus 로고    scopus 로고
    • Identification of a region at the N-terminus of phospholipase C-β3 that interacts with G protein βγ subunits
    • Barr A.J., Ali H., Haribabu B., Snyderman R., and Smrcka A.V. Identification of a region at the N-terminus of phospholipase C-β3 that interacts with G protein βγ subunits. Biochemistry 39 (2000) 1800-1806
    • (2000) Biochemistry , vol.39 , pp. 1800-1806
    • Barr, A.J.1    Ali, H.2    Haribabu, B.3    Snyderman, R.4    Smrcka, A.V.5
  • 36
    • 0030611335 scopus 로고    scopus 로고
    • 2+-dependent binding of calmodulin to an N-terminal motif of the heterotrimeric G protein β subunit
    • 2+-dependent binding of calmodulin to an N-terminal motif of the heterotrimeric G protein β subunit. J Biol Chem 272 (1997) 18801-18807
    • (1997) J Biol Chem , vol.272 , pp. 18801-18807
    • Liu, M.1    Yu, B.2    Nakanishi, O.3    Wieland, T.4    Simon, M.5
  • 37
    • 0025600997 scopus 로고
    • Distinct sequence elements control the specificity of G protein activation by musarnic acetylcholine receptor subtypes
    • Lechleiter J., Hellmiss R., Duerson K., Ennulat D., David N., Clapham D., et al. Distinct sequence elements control the specificity of G protein activation by musarnic acetylcholine receptor subtypes. EMBO 9 (1990) 4381-4390
    • (1990) EMBO , vol.9 , pp. 4381-4390
    • Lechleiter, J.1    Hellmiss, R.2    Duerson, K.3    Ennulat, D.4    David, N.5    Clapham, D.6
  • 38
    • 0024472066 scopus 로고    scopus 로고
    • Lechleiter J, Peralta E, Clapham D. Diverse functions of muscarinic acetylcholine receptor subtypes. Trends Pharmacol Sci 1989;Suppl:34-8.
  • 39
    • 0023773004 scopus 로고
    • Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes
    • Peralta E.G., Ashkenazi A., Winslow J.W., Ramachandran J., and Capon D.J. Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes. Nature 334 6181 (1988) 434-437
    • (1988) Nature , vol.334 , Issue.6181 , pp. 434-437
    • Peralta, E.G.1    Ashkenazi, A.2    Winslow, J.W.3    Ramachandran, J.4    Capon, D.J.5
  • 40
    • 0033538337 scopus 로고    scopus 로고
    • Phospholipase C-beta 1 directly accelerates GTP hydrolysis by Galpha q and acceleration is inhibited by Gbeta gamma subunits
    • Chidiac P., and Ross E.M. Phospholipase C-beta 1 directly accelerates GTP hydrolysis by Galpha q and acceleration is inhibited by Gbeta gamma subunits. J Biol Chem 274 28 (1999) 19639-23699
    • (1999) J Biol Chem , vol.274 , Issue.28 , pp. 19639-23699
    • Chidiac, P.1    Ross, E.M.2
  • 41
    • 0033605695 scopus 로고    scopus 로고
    • Identification of multiple phosphoinositide-specific phospholipases D as new regulatory enzymes for phosphatidylinositol 3,4,5-trisphosphate
    • Ching T.T., Wang D.S., Hsu A.L., Lu P.J., and Chen C.S. Identification of multiple phosphoinositide-specific phospholipases D as new regulatory enzymes for phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 274 13 (1999) 8611-8617
    • (1999) J Biol Chem , vol.274 , Issue.13 , pp. 8611-8617
    • Ching, T.T.1    Wang, D.S.2    Hsu, A.L.3    Lu, P.J.4    Chen, C.S.5
  • 44
    • 1842614409 scopus 로고    scopus 로고
    • PIP3 is involved in neuronal polarization and axon formation
    • Menager C., Arimura N., Fukata Y., and Kaibuchi K. PIP3 is involved in neuronal polarization and axon formation. J Neurochem 89 1 (2004) 109-118
    • (2004) J Neurochem , vol.89 , Issue.1 , pp. 109-118
    • Menager, C.1    Arimura, N.2    Fukata, Y.3    Kaibuchi, K.4
  • 45
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 and PIP3: complex roles at the cell surface
    • Czech M.P. PIP2 and PIP3: complex roles at the cell surface. Cell 100 6 (2000) 603-606
    • (2000) Cell , vol.100 , Issue.6 , pp. 603-606
    • Czech, M.P.1
  • 47
    • 23244454919 scopus 로고    scopus 로고
    • A targeted mass spectrometric analysis of phosphatidylinositol phosphate species
    • Milne S.B., Ivanova P.T., DeCamp D., Hsueh R.C., and Brown H.A. A targeted mass spectrometric analysis of phosphatidylinositol phosphate species. J Lipid Res 46 8 (2005) 1796-1802
    • (2005) J Lipid Res , vol.46 , Issue.8 , pp. 1796-1802
    • Milne, S.B.1    Ivanova, P.T.2    DeCamp, D.3    Hsueh, R.C.4    Brown, H.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.