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Volumn 257, Issue 1, 1998, Pages 236-241

Nonenzymatic palmitoylation at Cys 3 causes extra-activation of the α- subunit of the stimulatory GTP-binding protein G(s)

Author keywords

Hydroxylaminolysis; Nonenzymatic palmitoylation; Recombinant (s); Reconstitution

Indexed keywords

ADENYLATE CYCLASE; CYSTEINE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HYDROXYLAMINE; PALMITIC ACID; PROTEINASE;

EID: 0032190173     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570236.x     Document Type: Article
Times cited : (12)

References (32)
  • 1
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey, P. J. (1995) Protein lipidation in cell signaling, Science 268, 221-225.
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 3
    • 0029927840 scopus 로고    scopus 로고
    • G-protein palmitoyltransferase activity is enriched in plasma membranes
    • Dunphy, J. T., Greentree, W. K., Manahan, C. L. & Linder, M. E. (1996) G-protein palmitoyltransferase activity is enriched in plasma membranes, J. Biol. Chem. 271, 7154-7159.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7154-7159
    • Dunphy, J.T.1    Greentree, W.K.2    Manahan, C.L.3    Linder, M.E.4
  • 4
    • 0030890881 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a protein-palmitoyl acyltransferase from human erythrocytes
    • Das, A. K., Dasgupta, B., Bhattacharya, R. & Basu, J. (1997) Purification and biochemical characterization of a protein-palmitoyl acyltransferase from human erythrocytes, J. Biol. Chem. 272, 11021-11025.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11021-11025
    • Das, A.K.1    Dasgupta, B.2    Bhattacharya, R.3    Basu, J.4
  • 5
    • 0029789954 scopus 로고    scopus 로고
    • Purification of a protein palmitoyl-transferase that acts on H-Ras protein and on a C-terminal N-Ras peptide
    • Liu, L., Dudler, T. & Gelb, M. H. (1996) Purification of a protein palmitoyl-transferase that acts on H-Ras protein and on a C-terminal N-Ras peptide, J. Biol. Chem. 271, 23269-23276.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23269-23276
    • Liu, L.1    Dudler, T.2    Gelb, M.H.3
  • 6
    • 0029145798 scopus 로고
    • Biochemical characterization of a palmitoyl acyltransferase activity that palmitoylates myristoylated proteins
    • Berthiaume, L. & Resh, M. D. (1995) Biochemical characterization of a palmitoyl acyltransferase activity that palmitoylates myristoylated proteins, J. Biol. Chem. 270, 22399-22405.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22399-22405
    • Berthiaume, L.1    Resh, M.D.2
  • 10
    • 0029814190 scopus 로고    scopus 로고
    • Autoacylation of G protein alpha subunits
    • Duncan, J. A. & Gilman, A. G. (1996) Autoacylation of G protein alpha subunits, J. Biol. Chem. 271, 23594-23600.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23594-23600
    • Duncan, J.A.1    Gilman, A.G.2
  • 12
    • 0025117420 scopus 로고
    • A simple enzymatic method for the preparation of radiolabeled erucoyl-CoA and other long-chain fatty acyl-CoAs and their characterization by mass spectrometry
    • Taylor, D. C., Weber, N., Hogge, L. R. & Underhill, E. W. (1990) A simple enzymatic method for the preparation of radiolabeled erucoyl-CoA and other long-chain fatty acyl-CoAs and their characterization by mass spectrometry, Anal. Biochem. 184, 311-316.
    • (1990) Anal. Biochem. , vol.184 , pp. 311-316
    • Taylor, D.C.1    Weber, N.2    Hogge, L.R.3    Underhill, E.W.4
  • 14
    • 0025193724 scopus 로고
    • Identification of a Gs-protein coupling domain to the beta-adrenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gs alpha is involved in coupling to beta-adrenoceptors
    • Palm, D., Münch, G., Malek, D., Dees, C. & Hekman, M. (1990) Identification of a Gs-protein coupling domain to the beta-adrenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gs alpha is involved in coupling to beta-adrenoceptors, FEBS Lett. 261, 294-298.
    • (1990) FEBS Lett. , vol.261 , pp. 294-298
    • Palm, D.1    Münch, G.2    Malek, D.3    Dees, C.4    Hekman, M.5
  • 15
    • 0025951307 scopus 로고
    • Immuno-affinity purification and characterization of the alpha subunits of Go type G proteins from various bovine tissues
    • Asano, T., Morishita, R. & Kato, K. (1991) Immuno-affinity purification and characterization of the alpha subunits of Go type G proteins from various bovine tissues, J. Biochem. (Tokyo) 110, 571-574.
    • (1991) J. Biochem. (Tokyo) , vol.110 , pp. 571-574
    • Asano, T.1    Morishita, R.2    Kato, K.3
  • 16
    • 0022344176 scopus 로고
    • Relationships within the family of GTP-binding proteins isolated from bovine central nervous system
    • Roof, D. J., Applebury, M. L. & Sternweis, P. C. (1985) Relationships within the family of GTP-binding proteins isolated from bovine central nervous system, J. Biol. Chem. 260, 16242-16249.
    • (1985) J. Biol. Chem. , vol.260 , pp. 16242-16249
    • Roof, D.J.1    Applebury, M.L.2    Sternweis, P.C.3
  • 18
    • 0029160305 scopus 로고
    • Acylation of adenylyl cyclase catalyst is important for enzymic activity
    • Mollner, S., Beck, K. & Pfeuffer, T. (1995) Acylation of adenylyl cyclase catalyst is important for enzymic activity, FEBS Lett. 371, 241-244.
    • (1995) FEBS Lett. , vol.371 , pp. 241-244
    • Mollner, S.1    Beck, K.2    Pfeuffer, T.3
  • 19
    • 0028010777 scopus 로고
    • Molecular cloning and expression of a novel type V adenylyl cyclase from rabbit myocardium
    • Wallach, J., Droste, M., Kluxen, F. W., Pfeuffer, T. & Frank, R. (1994) Molecular cloning and expression of a novel type V adenylyl cyclase from rabbit myocardium, FEBS Lett. 338, 257-263.
    • (1994) FEBS Lett. , vol.338 , pp. 257-263
    • Wallach, J.1    Droste, M.2    Kluxen, F.W.3    Pfeuffer, T.4    Frank, R.5
  • 20
    • 0028672260 scopus 로고
    • Expression and purification of recombinant adenylyl cyclase in Sf9 cells
    • Taussig, R., Tang, W.-J. & Gilman, A. G. (1994) Expression and purification of recombinant adenylyl cyclase in Sf9 cells, Methods Enzymol. 238, 95-108.
    • (1994) Methods Enzymol. , vol.238 , pp. 95-108
    • Taussig, R.1    Tang, W.-J.2    Gilman, A.G.3
  • 21
  • 22
    • 0016213772 scopus 로고
    • Uncoupling of catecholamine activation of pigeon erythrocyte membrane adenylate cyclase by filipin
    • Puchwein, G., Pfeuffer, T. & Helmreich, E. J. M. (1974) Uncoupling of catecholamine activation of pigeon erythrocyte membrane adenylate cyclase by filipin, J. Biol. Chem. 249, 3232-3240.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3232-3240
    • Puchwein, G.1    Pfeuffer, T.2    Helmreich, E.J.M.3
  • 23
    • 0000010127 scopus 로고
    • 7-O-Hemisuccinyl-deacetyl forskolin-Sepharose: A novel affinity support for purification of adenylate cyclase
    • Pfeuffer, T. & Metzger, H. (1982) 7-O-Hemisuccinyl-deacetyl forskolin-Sepharose: a novel affinity support for purification of adenylate cyclase, FEBS Lett. 146, 369-375.
    • (1982) FEBS Lett. , vol.146 , pp. 369-375
    • Pfeuffer, T.1    Metzger, H.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0026463050 scopus 로고
    • The alpha subunit of the stimulatory guanine-nucleotide-binding regulatory protein forms high-molecular-mass aggregates, concomitant with iloprost-induced desensitization of human platelet adenylyl cyclase
    • Mollner, S., Deppisch, H. & Pfeuffer, T. (1992) The alpha subunit of the stimulatory guanine-nucleotide-binding regulatory protein forms high-molecular-mass aggregates, concomitant with iloprost-induced desensitization of human platelet adenylyl cyclase, Eur. J. Biochem. 210, 539-544.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 539-544
    • Mollner, S.1    Deppisch, H.2    Pfeuffer, T.3
  • 28
    • 0026744081 scopus 로고
    • Two members of a widely expressed subfamily of hormone-stimulated adenylyl cyclases
    • Premont, R. T., Chen, J., Ma, H. W., Ponnapalli, M. & Iyengar, R. (1992) Two members of a widely expressed subfamily of hormone-stimulated adenylyl cyclases, Proc. Natl Acad. Sci. USA 89, 9809-9813.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9809-9813
    • Premont, R.T.1    Chen, J.2    Ma, H.W.3    Ponnapalli, M.4    Iyengar, R.5
  • 29
    • 0027303086 scopus 로고
    • 3H]palmitic acid and mutation of cysteine-3 prevents this modification
    • 3H]palmitic acid and mutation of cysteine-3 prevents this modification, Biochemistry 32, 8057-8061.
    • (1993) Biochemistry , vol.32 , pp. 8057-8061
    • Degtyarev, M.Y.1    Spiegel, A.M.2    Jones, T.L.3
  • 31
    • 0030610232 scopus 로고    scopus 로고
    • Gs alpha contains an unidentified covalent modification that increases its affinity for adenylyl cyclase
    • Kleuss, C. & Gilman, A. G. (1997) Gs alpha contains an unidentified covalent modification that increases its affinity for adenylyl cyclase, Proc. Natl Acad. Sci. USA 94, 6116-6120.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6116-6120
    • Kleuss, C.1    Gilman, A.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.