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Volumn 64, Issue 1, 2003, Pages 11-20

Spatial regulation of Gαi protein signaling in clathrin-coated membrane microdomains containing GAIP

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN; DELTA OPIATE RECEPTOR; DYNAMIN; GALPHA INTERACTING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; RGS PROTEIN; RGS19 PROTEIN; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN; ADAPTOR PROTEIN; BACTERIAL PROTEIN; GNAI3 PROTEIN, HUMAN; GUANINE NUCLEOTIDE BINDING PROTEIN; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; PHOSPHOPROTEIN; PHOTOPROTEIN; REGULATOR OF G PROTEIN SIGNALLING 19; REGULATOR OF G-PROTEIN SIGNALLING 19; YELLOW FLUORESCENT PROTEIN, BACTERIA;

EID: 0038237084     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.64.1.11     Document Type: Article
Times cited : (28)

References (41)
  • 1
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson RGW (1998) The caveolae membrane system. Annu Rev Biochem 67:199-225.
    • (1998) Annu Rev Biochem , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 2
    • 0032933065 scopus 로고    scopus 로고
    • Immunocytochemical study of endocytic structures accumulated in HeLa cells transformed with a temperature-sensitive mutant of dynamin
    • Baba T, Ueda H, Terada N, Fujii Y, and Ohno S (1999) Immunocytochemical study of endocytic structures accumulated in HeLa cells transformed with a temperature-sensitive mutant of dynamin. J Histochem Cytochem 47:637-648.
    • (1999) J Histochem Cytochem , vol.47 , pp. 637-648
    • Baba, T.1    Ueda, H.2    Terada, N.3    Fujii, Y.4    Ohno, S.5
  • 4
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke H, Baba T, Warnock DE, and Schmid SL (1994) Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J Biol Chem 127:915-934.
    • (1994) J Biol Chem , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 6
    • 0030448762 scopus 로고    scopus 로고
    • GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Gαi subunits
    • De Vries L, Elenko E, Hubler L, Jones TL, and Farquhar MG (1996) GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Gαi subunits. Proc Natl Acad Sci USA 93:15203-15208.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15203-15208
    • De Vries, L.1    Elenko, E.2    Hubler, L.3    Jones, T.L.4    Farquhar, M.G.5
  • 8
    • 0029559788 scopus 로고
    • GAIP, a protein that specifically interacts with the trimeric G protein Gαi3, is a member of a protein family with a highly conserved core domain
    • De Vries L, Mousli M, Wurmser A, and Farquhar MG (1995) GAIP, a protein that specifically interacts with the trimeric G protein Gαi3, is a member of a protein family with a highly conserved core domain. Proc Natl Acad Sci USA 92:11916-11920.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11916-11920
    • De Vries, L.1    Mousli, M.2    Wurmser, A.3    Farquhar, M.G.4
  • 9
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson SSG (2001) Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol Rev 53:1-24.
    • (2001) Pharmacol Rev , vol.53 , pp. 1-24
    • Ferguson, S.S.G.1
  • 13
    • 0034463035 scopus 로고    scopus 로고
    • The rat gonadotropin-releasing hormone receptor internalizes via a beta-arrestin independent, but dynamin-dependent, pathway: Addition of a carboxyl-terminal tail confers beta-arrestin dependency
    • Heding A, Vrel M, Hanyalgolu AC, Sellar R, Taylore PL, and Eidne KA (2000) The rat gonadotropin-releasing hormone receptor internalizes via a beta-arrestin independent, but dynamin-dependent, pathway: addition of a carboxyl-terminal tail confers beta-arrestin dependency. Endocrinol 141:299-306.
    • (2000) Endocrinol , vol.141 , pp. 299-306
    • Heding, A.1    Vrel, M.2    Hanyalgolu, A.C.3    Sellar, R.4    Taylore, P.L.5    Eidne, K.A.6
  • 14
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw JE (2000) Dynamin and its role in membrane fission. Annu Rev Cell Dev Biol 16:483-519.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 17
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen E (2001) Roles of lipid rafts in membrane transport. Curr Opin Cell Biol 13:470-477.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 18
    • 0027435603 scopus 로고
    • Topological mechanisms involved in the formation of clathrin-coated vesicles
    • Jin A and Nossal R (1993) Topological mechanisms involved in the formation of clathrin-coated vesicles. Biophys J 65:1523-1537.
    • (1993) Biophys J , vol.65 , pp. 1523-1537
    • Jin, A.1    Nossal, R.2
  • 19
    • 0033520914 scopus 로고    scopus 로고
    • Activation of Src family kinase Yes induced by shiga toxin binding to globotriaosyl ceramide (Gb3/CD77) in low density, detergent-insoluble microdomains
    • Katagiri YU, Mori T, Nakajima MT, Katagiri C, Taguchi T, Takeda T, Kiyokawa N and Fujimoto J (1999) Activation of Src family kinase Yes induced by shiga toxin binding to globotriaosyl ceramide (Gb3/CD77) in low density, detergent-insoluble microdomains. J Biol Chem 274:35278-35282.
    • (1999) J Biol Chem , vol.274 , pp. 35278-35282
    • Katagiri, Y.U.1    Mori, T.2    Nakajima, M.T.3    Katagiri, C.4    Taguchi, T.5    Takeda, T.6    Kiyokawa, N.7    Fujimoto, J.8
  • 21
    • 0026474549 scopus 로고
    • Activation of the alpha subunit of Gs in intact cells alters its abundance, rate of degradation and membrane avidity
    • Levis M and Bourne H (1992) Activation of the alpha subunit of Gs in intact cells alters its abundance, rate of degradation and membrane avidity. J Cell Biol 119:1297-1307.
    • (1992) J Cell Biol , vol.119 , pp. 1297-1307
    • Levis, M.1    Bourne, H.2
  • 22
    • 0033538576 scopus 로고    scopus 로고
    • The structural era of endocytosis
    • Marsh M and McMahon HT (1999) The structural era of endocytosis. Science (Wash DC) 285:215-219.
    • (1999) Science (Wash DC) , vol.285 , pp. 215-219
    • Marsh, M.1    McMahon, H.T.2
  • 24
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • Moffett S, Brown DA, and Linder ME (2000) Lipid-dependent targeting of G proteins into rafts. J Biol Chem 275:2191-2198.
    • (2000) J Biol Chem , vol.275 , pp. 2191-2198
    • Moffett, S.1    Brown, D.A.2    Linder, M.E.3
  • 25
    • 0029030937 scopus 로고
    • EEA1, an early endosome-associated protein. EEA1 is a conserved α-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif
    • Mu FT, Callaghan JM, Steele-Mortimer O, Stenmark H, Parton RG, Campbell PL, McCluskey J, Yeo JP, Tock EP, and Toh BH (1995) EEA1, an early endosome-associated protein. EEA1 is a conserved α-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif. J Biol Chem 270:13503-13511.
    • (1995) J Biol Chem , vol.270 , pp. 13503-13511
    • Mu, F.T.1    Callaghan, J.M.2    Steele-Mortimer, O.3    Stenmark, H.4    Parton, R.G.5    Campbell, P.L.6    McCluskey, J.7    Yeo, J.P.8    Tock, E.P.9    Toh, B.H.10
  • 26
    • 0032566523 scopus 로고    scopus 로고
    • Phosphorylation is not required for dynamin-dependent endocytosis of a truncated mutant opioid receptor
    • Murray SR, Evans CJ, and von Zastrow M (1998) Phosphorylation is not required for dynamin-dependent endocytosis of a truncated mutant opioid receptor. J Biol Chem 273:24987-24991.
    • (1998) J Biol Chem , vol.273 , pp. 24987-24991
    • Murray, S.R.1    Evans, C.J.2    Von Zastrow, M.3
  • 27
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig RR (1994) Membrane organization in G-protein mechanisms. Faseb J 8:939-946.
    • (1994) Faseb J , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 28
    • 0032931988 scopus 로고    scopus 로고
    • Extraction of cholesterol with methyl-β-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles
    • Rodal SK, Skretting G, Garred O, Vilhardt F, Deurs B, and Sandvig K (1999) Extraction of cholesterol with methyl-β-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles. Mol Biol Cell 10:961-974.
    • (1999) Mol Biol Cell , vol.10 , pp. 961-974
    • Rodal, S.K.1    Skretting, G.2    Garred, O.3    Vilhardt, F.4    Deurs, B.5    Sandvig, K.6
  • 29
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins
    • Ross EM and Wilkie TM (2000) GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu Rev Biochem 69:795-827.
    • (2000) Annu Rev Biochem , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2
  • 30
    • 0031765341 scopus 로고    scopus 로고
    • Role of plasmalemmal caveolae in signal transduction
    • Shaul PW and Anderson RG (1998) Role of plasmalemmal caveolae in signal transduction. Am J Physiol 275:L843-L851.
    • (1998) Am J Physiol , vol.275
    • Shaul, P.W.1    Anderson, R.G.2
  • 31
    • 0035937752 scopus 로고    scopus 로고
    • Cholera toxin is found in detergent-insoluble rafts/domains at the cell surface of hippocampal neurons but is internalized via a raft-independent mechanism
    • Shogomori H and Futerman AH (2001) Cholera toxin is found in detergent-insoluble rafts/domains at the cell surface of hippocampal neurons but is internalized via a raft-independent mechanism. J Biol Chem 276:9182-9188.
    • (2001) J Biol Chem , vol.276 , pp. 9182-9188
    • Shogomori, H.1    Futerman, A.H.2
  • 32
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K and Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1:31-41.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-41
    • Simons, K.1    Toomre, D.2
  • 33
    • 0035029169 scopus 로고    scopus 로고
    • Compartmentation of G protein-coupled signaling pathways in cardiac myocytes
    • Steinberg SF and Brunton LL (2001) Compartmentation of G protein-coupled signaling pathways in cardiac myocytes. Annu Rev Pharmacol Toxicol 41:751-773.
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 751-773
    • Steinberg, S.F.1    Brunton, L.L.2
  • 35
    • 0034646719 scopus 로고    scopus 로고
    • Type-specific sorting of G protein-coupled receptors after endocytosis
    • Tsao PI and von Zastrow M (2000) Type-specific sorting of G protein-coupled receptors after endocytosis. J Biol Chem 275:1130-1140.
    • (2000) J Biol Chem , vol.275 , pp. 1130-1140
    • Tsao, P.I.1    Von Zastrow, M.2
  • 36
    • 0035055204 scopus 로고    scopus 로고
    • Diversity and specificity in the regulated endocytic membrane trafficking of G-protein-coupled receptors
    • Tsao PI and von Zastrow M (2001) Diversity and specificity in the regulated endocytic membrane trafficking of G-protein-coupled receptors. Pharmacol Ther 89:139-147.
    • (2001) Pharmacol Ther , vol.89 , pp. 139-147
    • Tsao, P.I.1    Von Zastrow, M.2
  • 37
    • 0031752275 scopus 로고    scopus 로고
    • Lipid modifications and membrane targeting of G alpha
    • Wedegaertner PB (1998) Lipid modifications and membrane targeting of G alpha. Biol Signals Recept 7:125-135.
    • (1998) Biol Signals Recept , vol.7 , pp. 125-135
    • Wedegaertner, P.B.1
  • 38
    • 0029779537 scopus 로고    scopus 로고
    • Activation-induced subcellular redistribution of Gs alpha
    • Wedegaertner PB, Bourne HR, and von Zastrow M (1996) Activation-induced subcellular redistribution of Gs alpha. Mol Biol Cell 7:1225-1233.
    • (1996) Mol Biol Cell , vol.7 , pp. 1225-1233
    • Wedegaertner, P.B.1    Bourne, H.R.2    Von Zastrow, M.3
  • 39
    • 0035909784 scopus 로고    scopus 로고
    • Gαi3 binding to calnuc on Golgi membranes in living cells monitored by fluorescence resonance energy transfer of green fluorescent protein fusion proteins
    • Weiss TS, Chamberlain CE, Takeda T, Lin P, Hahn KM, and Farquhar MG (2001) Gαi3 binding to calnuc on Golgi membranes in living cells monitored by fluorescence resonance energy transfer of green fluorescent protein fusion proteins. Proc Natl Acad Sci USA 98:14961-14966.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14961-14966
    • Weiss, T.S.1    Chamberlain, C.E.2    Takeda, T.3    Lin, P.4    Hahn, K.M.5    Farquhar, M.G.6
  • 40
    • 0035823533 scopus 로고    scopus 로고
    • A Phosphorylation-regulated brake mechanism controls the initial endocytosis of opioid receptors but is not required for post-endocytic sorting to lysosomes
    • Whistler JL, Tsao PI, and von Zastrow M (2001) A Phosphorylation-regulated brake mechanism controls the initial endocytosis of opioid receptors but is not required for post-endocytic sorting to lysosomes. J Biol Chem 276:34331-34388.
    • (2001) J Biol Chem , vol.276 , pp. 34331-34388
    • Whistler, J.L.1    Tsao, P.I.2    Von Zastrow, M.3
  • 41
    • 0036151483 scopus 로고    scopus 로고
    • αs: Dissociation of the activated G protein from plasma membrane
    • αs: dissociation of the activated G protein from plasma membrane. Mol Pharmacol 61:352-359.
    • (2002) Mol Pharmacol , vol.61 , pp. 352-359
    • Yu, J.Z.1    Rasenick, M.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.