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Volumn 109, Issue 51, 2012, Pages

G-protein signaling leverages subunit-dependent membrane affinity to differentially control βγ translocation to intracellular membranes

Author keywords

G protein coupled receptors; Protein membrane interaction; Spatio temporal dynamics

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 84871373858     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1205345109     Document Type: Article
Times cited : (40)

References (51)
  • 1
    • 77955838654 scopus 로고    scopus 로고
    • Spatial cycles in G-protein crowd control
    • Vartak N, Bastiaens P (2010) Spatial cycles in G-protein crowd control. EMBO J 29(16):2689-2699.
    • (2010) EMBO J , vol.29 , Issue.16 , pp. 2689-2699
    • Vartak, N.1    Bastiaens, P.2
  • 2
    • 23744505102 scopus 로고    scopus 로고
    • Reversible intracellular translocation of KRas but not HRas in hippocampal neurons regulated by Ca2+/calmodulin
    • Fivaz M, Meyer T (2005) Reversible intracellular translocation of KRas but not HRas in hippocampal neurons regulated by Ca2+/calmodulin. J Cell Biol 170(3):429-441.
    • (2005) J Cell Biol , vol.170 , Issue.3 , pp. 429-441
    • Fivaz, M.1    Meyer, T.2
  • 3
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • Hamm HE (1998) The many faces of G protein signaling. J Biol Chem 273(2):669-672.
    • (1998) J Biol Chem , vol.273 , Issue.2 , pp. 669-672
    • Hamm, H.E.1
  • 4
    • 10944232035 scopus 로고    scopus 로고
    • Receptor-mediated reversible translocation of the G protein betagamma complex from the plasma membrane to the Golgi complex
    • Akgoz M, Kalyanaraman V, Gautam N (2004) Receptor-mediated reversible translocation of the G protein betagamma complex from the plasma membrane to the Golgi complex. J Biol Chem 279(49):51541-51544.
    • (2004) J Biol Chem , vol.279 , Issue.49 , pp. 51541-51544
    • Akgoz, M.1    Kalyanaraman, V.2    Gautam, N.3
  • 5
    • 33646342993 scopus 로고    scopus 로고
    • G protein betagamma11 complex translocation is induced by Gi, Gq and Gs coupling receptors and is regulated by the alpha subunit type
    • Azpiazu I, Akgoz M, Kalyanaraman V, Gautam N (2006) G protein betagamma11 complex translocation is induced by Gi, Gq and Gs coupling receptors and is regulated by the alpha subunit type. Cell Signal 18(8):1190-1200.
    • (2006) Cell Signal , vol.18 , Issue.8 , pp. 1190-1200
    • Azpiazu, I.1    Akgoz, M.2    Kalyanaraman, V.3    Gautam, N.4
  • 6
    • 34548238232 scopus 로고    scopus 로고
    • A family of G protein βγ subunits translocate reversibly from the plasma membrane to endomembranes on receptor activation
    • Saini DK, Kalyanaraman V, Chisari M, Gautam N (2007) A family of G protein βγ subunits translocate reversibly from the plasma membrane to endomembranes on receptor activation. J Biol Chem 282(33):24099-24108.
    • (2007) J Biol Chem , vol.282 , Issue.33 , pp. 24099-24108
    • Saini, D.K.1    Kalyanaraman, V.2    Chisari, M.3    Gautam, N.4
  • 7
    • 48949120507 scopus 로고    scopus 로고
    • Differential dissociation of G protein heterotrimers
    • Digby GJ, Sethi PR, Lambert NA (2008) Differential dissociation of G protein heterotrimers. J Physiol 586(14):3325-3335.
    • (2008) J Physiol , vol.586 , Issue.14 , pp. 3325-3335
    • Digby, G.J.1    Sethi, P.R.2    Lambert, N.A.3
  • 9
  • 10
    • 0028968896 scopus 로고
    • Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes
    • Shahinian S, Silvius JR (1995) Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes. Biochemistry 34(11):3813-3822.
    • (1995) Biochemistry , vol.34 , Issue.11 , pp. 3813-3822
    • Shahinian, S.1    Silvius, J.R.2
  • 11
    • 0028196986 scopus 로고
    • Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers
    • Silvius JR, l'Heureux F (1994) Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry 33(10):3014-3022.
    • (1994) Biochemistry , vol.33 , Issue.10 , pp. 3014-3022
    • Silvius, J.R.1    L'Heureux, F.2
  • 12
    • 30044431691 scopus 로고    scopus 로고
    • K-ras4B and prenylated proteins lacking "second signals" associate dynamically with cellular membranes
    • Silvius JR, Bhagatji P, Leventis R, Terrone D (2006) K-ras4B and prenylated proteins lacking "second signals" associate dynamically with cellular membranes. Mol Biol Cell 17(1):192-202.
    • (2006) Mol Biol Cell , vol.17 , Issue.1 , pp. 192-202
    • Silvius, J.R.1    Bhagatji, P.2    Leventis, R.3    Terrone, D.4
  • 13
    • 33747065335 scopus 로고    scopus 로고
    • G protein betagamma complex translocation from plasma membrane to Golgi complex is influenced by receptor gamma subunit interaction
    • Akgoz M, Kalyanaraman V, Gautam N (2006) G protein betagamma complex translocation from plasma membrane to Golgi complex is influenced by receptor gamma subunit interaction. Cell Signal 18(10):1758-1768.
    • (2006) Cell Signal , vol.18 , Issue.10 , pp. 1758-1768
    • Akgoz, M.1    Kalyanaraman, V.2    Gautam, N.3
  • 14
    • 0026009360 scopus 로고
    • G-protein beta gamma dimers. Membrane targeting requires subunit coexpression and intact gamma C-A-A-X domain
    • Simonds WF, Butrynski JE, Gautam N, Unson CG, Spiegel AM (1991) G-protein beta gamma dimers. Membrane targeting requires subunit coexpression and intact gamma C-A-A-X domain. J Biol Chem 266(9):5363-5366.
    • (1991) J Biol Chem , vol.266 , Issue.9 , pp. 5363-5366
    • Simonds, W.F.1    Butrynski, J.E.2    Gautam, N.3    Unson, C.G.4    Spiegel, A.M.5
  • 15
    • 33846637432 scopus 로고    scopus 로고
    • Kinetic diversity in G-protein-coupled receptor signalling
    • Katanaev VL, Chornomorets M (2007) Kinetic diversity in G-protein-coupled receptor signalling. Biochem J 401(2):485-495.
    • (2007) Biochem J , vol.401 , Issue.2 , pp. 485-495
    • Katanaev, V.L.1    Chornomorets, M.2
  • 16
    • 0032546549 scopus 로고    scopus 로고
    • Lipid-binding characteristics of the polybasic carboxyterminal sequence of K-ras4B
    • Leventis R, Silvius JR (1998) Lipid-binding characteristics of the polybasic carboxyterminal sequence of K-ras4B. Biochemistry 37(20):7640-7648.
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7640-7648
    • Leventis, R.1    Silvius, J.R.2
  • 17
    • 78649263874 scopus 로고    scopus 로고
    • Multiple cellular proteins modulate the dynamics of K-ras association with the plasma membrane
    • Bhagatji P, Leventis R, Rich R, Lin CJ, Silvius JR (2010) Multiple cellular proteins modulate the dynamics of K-ras association with the plasma membrane. Biophys J 99(10):3327 - 3335.
    • (2010) Biophys J , vol.99 , Issue.10 , pp. 3327-3335
    • Bhagatji, P.1    Leventis, R.2    Rich, R.3    Lin, C.J.4    Silvius, J.R.5
  • 18
    • 57649178347 scopus 로고    scopus 로고
    • Electrostatic and lipid anchor contributions to the interaction of transducin with membranes: Mechanistic implications for activation and translocation
    • Kosloff M, Alexov E, Arshavsky VY, Honig B (2008) Electrostatic and lipid anchor contributions to the interaction of transducin with membranes: Mechanistic implications for activation and translocation. J Biol Chem 283(45):31197-31207.
    • (2008) J Biol Chem , vol.283 , Issue.45 , pp. 31197-31207
    • Kosloff, M.1    Alexov, E.2    Arshavsky, V.Y.3    Honig, B.4
  • 19
    • 77956539715 scopus 로고    scopus 로고
    • Size dependence of protein diffusion in the cytoplasm of Escherichia coli
    • Nenninger A, Mastroianni G, Mullineaux CW (2010) Size dependence of protein diffusion in the cytoplasm of Escherichia coli. J Bacteriol 192(18):4535- 4540.
    • (2010) J Bacteriol , vol.192 , Issue.18 , pp. 4535-4540
    • Nenninger, A.1    Mastroianni, G.2    Mullineaux, C.W.3
  • 20
    • 79960706295 scopus 로고    scopus 로고
    • The 'invisible hand': Regulation of RHO GTPases by RHOGDIs
    • Garcia-Mata R, Boulter E, Burridge K (2011) The 'invisible hand': Regulation of RHO GTPases by RHOGDIs. Nat Rev Mol Cell Biol 12(8):493-504.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.8 , pp. 493-504
    • Garcia-Mata, R.1    Boulter, E.2    Burridge, K.3
  • 21
    • 8444243363 scopus 로고    scopus 로고
    • Targeting Rab GTPases to distinct membrane compartments
    • Pfeffer S, Aivazian D (2004) Targeting Rab GTPases to distinct membrane compartments. Nat RevMol Cell Biol 5(11):886-896.
    • (2004) Nat RevMol Cell Biol , vol.5 , Issue.11 , pp. 886-896
    • Pfeffer, S.1    Aivazian, D.2
  • 22
    • 81355127367 scopus 로고    scopus 로고
    • Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo
    • Ismail SA, et al. (2011) Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. Nat Chem Biol 7(12):942-949.
    • (2011) Nat Chem Biol , vol.7 , Issue.12 , pp. 942-949
    • Ismail, S.A.1
  • 23
    • 2442433666 scopus 로고    scopus 로고
    • Phosducin facilitates light-driven transducin translocation in rod photoreceptors. Evidence from the phosducin knockout mouse
    • Sokolov M, et al. (2004) Phosducin facilitates light-driven transducin translocation in rod photoreceptors. Evidence from the phosducin knockout mouse. J Biol Chem 279(18):19149-19156.
    • (2004) J Biol Chem , vol.279 , Issue.18 , pp. 19149-19156
    • Sokolov, M.1
  • 24
    • 0035977019 scopus 로고    scopus 로고
    • The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers
    • Murray D, McLaughlin S, Honig B (2001) The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers. J Biol Chem 276(48):45153- 45159.
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 45153-45159
    • Murray, D.1    McLaughlin, S.2    Honig, B.3
  • 25
    • 0032872786 scopus 로고    scopus 로고
    • Amphitropic proteins: Regulation by reversible membrane interactions
    • review
    • Johnson JE, Cornell RB (1999) Amphitropic proteins: Regulation by reversible membrane interactions (review). Mol Membr Biol 16(3):217-235.
    • (1999) Mol Membr Biol , vol.16 , Issue.3 , pp. 217-235
    • Johnson, J.E.1    Cornell, R.B.2
  • 26
    • 44149092177 scopus 로고    scopus 로고
    • Membranes: A meeting point for lipids, proteins and therapies
    • Escribá PV, et al. (2008) Membranes: A meeting point for lipids, proteins and therapies. J Cell Mol Med 12(3):829-875.
    • (2008) J Cell Mol Med , vol.12 , Issue.3 , pp. 829-875
    • Escribá, P.V.1
  • 27
    • 61749103498 scopus 로고    scopus 로고
    • Ras subcellular localization defines extracellular signal-regulated kinase 1 and 2 substrate specificity through distinct utilization of scaffold proteins
    • Casar B, et al. (2009) Ras subcellular localization defines extracellular signal-regulated kinase 1 and 2 substrate specificity through distinct utilization of scaffold proteins. Mol Cell Biol 29(5):1338-1353.
    • (2009) Mol Cell Biol , vol.29 , Issue.5 , pp. 1338-1353
    • Casar, B.1
  • 28
    • 73349139547 scopus 로고    scopus 로고
    • Cell fate decisions are specified by the dynamic ERK interactome
    • von Kriegsheim A, et al. (2009) Cell fate decisions are specified by the dynamic ERK interactome. Nat Cell Biol 11(12):1458-1464.
    • (2009) Nat Cell Biol , vol.11 , Issue.12 , pp. 1458-1464
    • Von Kriegsheim, A.1
  • 30
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • Cho WH, Stahelin RV (2005) Membrane-protein interactions in cell signaling and membrane trafficking. Annu Rev Biophys Biomol Struct 34:119-151.
    • (2005) Annu Rev Biophys Biomol Struct , vol.34 , pp. 119-151
    • Cho, W.H.1    Stahelin, R.V.2
  • 31
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • Resh MD (2006) Trafficking and signaling by fatty-acylated and prenylated proteins. Nat Chem Biol 2(11):584-590.
    • (2006) Nat Chem Biol , vol.2 , Issue.11 , pp. 584-590
    • Resh, M.D.1
  • 32
    • 0028234577 scopus 로고
    • N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization
    • Cadwallader KA, Paterson H, Macdonald SG, Hancock JF (1994) N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization. Mol Cell Biol 14(7):4722-4730.
    • (1994) Mol Cell Biol , vol.14 , Issue.7 , pp. 4722-4730
    • Cadwallader, K.A.1    Paterson, H.2    Macdonald, S.G.3    Hancock, J.F.4
  • 33
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock JF, Paterson H, Marshall CJ (1990) A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 63(1):133-139.
    • (1990) Cell , vol.63 , Issue.1 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 34
    • 0030250003 scopus 로고    scopus 로고
    • Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins
    • Resh MD (1996) Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins. Cell Signal 8(6):403-412.
    • (1996) Cell Signal , vol.8 , Issue.6 , pp. 403-412
    • Resh, M.D.1
  • 35
    • 0030696229 scopus 로고    scopus 로고
    • S-Acylation and plasma membrane targeting of the farnesylated carboxyl-terminal peptide of N-ras in mammalian fibroblasts
    • Schroeder H, et al. (1997) S-Acylation and plasma membrane targeting of the farnesylated carboxyl-terminal peptide of N-ras in mammalian fibroblasts. Biochemistry 36(42):13102-13109.
    • (1997) Biochemistry , vol.36 , Issue.42 , pp. 13102-13109
    • Schroeder, H.1
  • 36
    • 0036732940 scopus 로고    scopus 로고
    • Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi
    • Michaelson D, Ahearn I, Bergo M, Young S, Philips M (2002) Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi. Mol Biol Cell 13(9):3294-3302.
    • (2002) Mol Biol Cell , vol.13 , Issue.9 , pp. 3294-3302
    • Michaelson, D.1    Ahearn, I.2    Bergo, M.3    Young, S.4    Philips, M.5
  • 37
    • 0038607927 scopus 로고    scopus 로고
    • Heterotrimer formation, together with isoprenylation, is required for plasma membrane targeting of Gbetagamma
    • Takida S, Wedegaertner PB (2003) Heterotrimer formation, together with isoprenylation, is required for plasma membrane targeting of Gbetagamma. J Biol Chem 278(19):17284-17290.
    • (2003) J Biol Chem , vol.278 , Issue.19 , pp. 17284-17290
    • Takida, S.1    Wedegaertner, P.B.2
  • 40
    • 33746503286 scopus 로고    scopus 로고
    • Receptor activation alters inner surface potential during phagocytosis
    • Yeung T, et al. (2006) Receptor activation alters inner surface potential during phagocytosis. Science 313(5785):347-351.
    • (2006) Science , vol.313 , Issue.5785 , pp. 347-351
    • Yeung, T.1
  • 41
    • 20144375061 scopus 로고    scopus 로고
    • An acylation cycle regulates localization and activity of palmitoylated Ras isoforms
    • Rocks O, et al. (2005) An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science 307(5716):1746-1752.
    • (2005) Science , vol.307 , Issue.5716 , pp. 1746-1752
    • Rocks, O.1
  • 42
    • 22944460791 scopus 로고    scopus 로고
    • Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway
    • Goodwin JS, et al. (2005) Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway. J Cell Biol 170(2):261-272.
    • (2005) J Cell Biol , vol.170 , Issue.2 , pp. 261-272
    • Goodwin, J.S.1
  • 43
    • 84856492497 scopus 로고    scopus 로고
    • The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins
    • Chandra A, et al. (2012) The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins. Nat Cell Biol 14(2):148-158.
    • (2012) Nat Cell Biol , vol.14 , Issue.2 , pp. 148-158
    • Chandra, A.1
  • 44
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: Central regulatory molecules in Rho GTPase activation
    • DerMardirossian C, Bokoch GM (2005) GDIs: Central regulatory molecules in Rho GTPase activation. Trends Cell Biol 15(7):356-363.
    • (2005) Trends Cell Biol , vol.15 , Issue.7 , pp. 356-363
    • DerMardirossian, C.1    Bokoch, G.M.2
  • 45
    • 77954937492 scopus 로고    scopus 로고
    • Regulation of Golgi structure and secretion by receptor-induced G protein βγ complex translocation
    • Saini DK, et al. (2010) Regulation of Golgi structure and secretion by receptor-induced G protein βγ complex translocation. Proc Natl Acad Sci USA 107(25):11417-11422.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.25 , pp. 11417-11422
    • Saini, D.K.1
  • 46
    • 79951850682 scopus 로고    scopus 로고
    • Alteration of Golgi structure in senescent cells and its regulation by a G protein γ subunit
    • Cho JH, Saini DK, Karunarathne WKA, Kalyanaraman V, Gautam N (2011) Alteration of Golgi structure in senescent cells and its regulation by a G protein γ subunit. Cell Signal 23(5):785-793.
    • (2011) Cell Signal , vol.23 , Issue.5 , pp. 785-793
    • Cho, J.H.1    Saini, D.K.2    Karunarathne, W.K.A.3    Kalyanaraman, V.4    Gautam, N.5
  • 47
    • 80755132220 scopus 로고    scopus 로고
    • Non-canonical signaling and localizations of heterotrimeric G proteins
    • Hewavitharana T, Wedegaertner PB (2012) Non-canonical signaling and localizations of heterotrimeric G proteins. Cell Signal 24(1):25-34.
    • (2012) Cell Signal , vol.24 , Issue.1 , pp. 25-34
    • Hewavitharana, T.1    Wedegaertner, P.B.2
  • 48
    • 0025132866 scopus 로고
    • Solution phase synthesis of Saccharomyces cerevisiae a-mating factor and its analogs
    • Xue CB, Ewenson A, Becker JM, Naider F (1990) Solution phase synthesis of Saccharomyces cerevisiae a-mating factor and its analogs. Int J Pept Protein Res 36(4):362-373.
    • (1990) Int J Pept Protein Res , vol.36 , Issue.4 , pp. 362-373
    • Xue, C.B.1    Ewenson, A.2    Becker, J.M.3    Naider, F.4
  • 49
    • 0025893761 scopus 로고
    • Synthesis of S-alkyl and C-terminal analogs of the Saccharomyces cerevisiae a-factor. Influence of temperature on the stability of Fmoc and OFm groups toward HF
    • Xue CB, Becker JM, Naider F (1991) Synthesis of S-alkyl and C-terminal analogs of the Saccharomyces cerevisiae a-factor. Influence of temperature on the stability of Fmoc and OFm groups toward HF. Int J Pept Protein Res 37(6):476-486.
    • (1991) Int J Pept Protein Res , vol.37 , Issue.6 , pp. 476-486
    • Xue, C.B.1    Becker, J.M.2    Naider, F.3
  • 50
    • 70349277032 scopus 로고    scopus 로고
    • COMU: A safer and more effective replacement for benzotriazole-based uronium coupling reagents
    • El-Faham A, Subirós Funosas R, Prohens R, Albericio F (2009) COMU: A safer and more effective replacement for benzotriazole-based uronium coupling reagents. Chemistry 15(37):9404-9416.
    • (2009) Chemistry , vol.15 , Issue.37 , pp. 9404-9416
    • El-Faham, A.1    Subirós Funosas, R.2    Prohens, R.3    Albericio, F.4
  • 51
    • 0035896201 scopus 로고    scopus 로고
    • Acid-labile protecting groups for the synthesis of lipidated peptides
    • Kadereit D, Deck P, Heinemann I, Waldmann H (2001) Acid-labile protecting groups for the synthesis of lipidated peptides. Chemistry 7(6):1184-1193.
    • (2001) Chemistry , vol.7 , Issue.6 , pp. 1184-1193
    • Kadereit, D.1    Deck, P.2    Heinemann, I.3    Waldmann, H.4


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