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Volumn 136, Issue 5, 1997, Pages

Rapid plasma membrane anchoring of newly synthesized p59(fyn): Selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine- 3

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTEINE; DETERGENT; MEMBRANE PROTEIN; MESSENGER RNA; METHIONINE; MYRISTIC ACID; PALMITIC ACID; PROTEIN TYROSINE KINASE;

EID: 84866476582     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.136.5.1023     Document Type: Article
Times cited : (125)

References (57)
  • 3
    • 0029145798 scopus 로고
    • Biochemical characterization of a palmitoyl acyltransferase activity that palmiloylates myristylated proteins
    • Berthiaume, L., and M.D. Resh. 1995. Biochemical characterization of a palmitoyl acyltransferase activity that palmiloylates myristylated proteins. J. Biol. Chem. 270:22399-22405.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22399-22405
    • Berthiaume, L.1    Resh, M.D.2
  • 6
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey, P.J. 1995. Protein lipidation in cell signaling. Science (Wash. DC). 268:221-225.
    • (1995) Science (Wash. DC) , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 8
    • 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
  • 11
    • 0029814190 scopus 로고    scopus 로고
    • Autoacylation of G protein a subunits
    • Duncan, J.A., and A.G. Gilman. 1996. Autoacylation of G protein a 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
    • 0029927840 scopus 로고    scopus 로고
    • G-protein palmitoyltransferase activity is enriched in plasma membranes
    • Dunphy, J.T., W.K. Greentree, C.L. Manahan, and M.E. Linder. 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
  • 13
    • 0007443841 scopus 로고
    • Translational diffusion of membrane proteins
    • P. Yeagle. editor. CRC Press Ins., Boca Raton, FL.
    • Edidin, M. 1991. Translational diffusion of membrane proteins. In The Structure of Biological Membranes. P. Yeagle. editor. CRC Press Ins., Boca Raton, FL. 539-572.
    • (1991) The Structure of Biological Membranes , pp. 539-572
    • Edidin, M.1
  • 14
    • 0027332995 scopus 로고
    • Cloning of a TGFβ type I receptor that forms heteromeric complex with the TGFβ type II receptor
    • Franzen, P., P. ten Dijke, H. Ichijo, H. Yamashita, P. Schutz, C.-H. Heldin, and K. Miyazono. 1993. Cloning of a TGFβ type I receptor that forms heteromeric complex with the TGFβ type II receptor. Cell. 75:681-692
    • (1993) Cell , vol.75 , pp. 681-692
    • Franzen, P.1    Ten Dijke, P.2    Ichijo, H.3    Yamashita, H.4    Schutz, P.5    Heldin, C.-H.6    Miyazono, K.7
  • 15
    • 0026515961 scopus 로고
    • fyn is associated with the T cell receptor-CD3 complex in functional human lymphocytes
    • fyn is associated with the T cell receptor-CD3 complex in functional human lymphocytes. Eur. J. Immunol. 22:283-286.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 283-286
    • Gassmann, M.1    Guttinger, M.2    Amrein, K.E.3    Burn, P.4
  • 16
    • 0028170814 scopus 로고
    • Role of protein modification reactions in programming interactions between Ras-related GTP-asesmd cell membranes
    • Glomset, J.A., and C.C. Farnsworth. 1994. Role of protein modification reactions in programming interactions between Ras-related GTP-asesmd cell membranes. Annu. Rev. Cell Biol. 10:181-205.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 181-205
    • Glomset, J.A.1    Farnsworth, C.C.2
  • 17
    • 0023317189 scopus 로고
    • src with Triton X-100-resistant cellular structure correlates with morphological transfer mation
    • src with Triton X-100-resistant cellular structure correlates with morphological transfer mation. Proc. Natl. Acad. Sci. USA. 84:2313-2316.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2313-2316
    • Hamaguchi, M.1    Hanafusa, H.2
  • 18
    • 0028023828 scopus 로고
    • Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function
    • Hartson, S.D., and R.L. Matts. 1994. Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function. Biochemistry. 33:8912-8920.
    • (1994) Biochemistry , vol.33 , pp. 8912-8920
    • Hartson, S.D.1    Matts, R.L.2
  • 19
    • 0025306167 scopus 로고
    • Fatty acylated proteins as components of intracellular signaling pathways
    • James, G., and E.N. Olson. 1990. Fatty acylated proteins as components of intracellular signaling pathways. Biochemistry. 29:2623-2634.
    • (1990) Biochemistry , vol.29 , pp. 2623-2634
    • James, G.1    Olson, E.N.2
  • 24
    • 0029076816 scopus 로고
    • Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum
    • Lauring, B., H. Sakai, G. Kreibich, and M. Wiedmann. 1995. Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 92:5411-5414.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5411-5414
    • Lauring, B.1    Sakai, H.2    Kreibich, G.3    Wiedmann, M.4
  • 25
    • 0018718444 scopus 로고
    • Virus-specific messenger RNAs in permissive cells infected by avian sarcoma virus
    • Lee, J.S., H.E. Varmus, and J.M. Bishop. 1979. Virus-specific messenger RNAs in permissive cells infected by avian sarcoma virus. J. Biol. Chem. 254:8015-8022.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8015-8022
    • Lee, J.S.1    Varmus, H.E.2    Bishop, J.M.3
  • 27
    • 0028279060 scopus 로고
    • Distinct intracellular localization of Lck and Fyn protein tyrosine kinases in human T-lymphocytes
    • Ley, S.C., M. Marsh, C.R. Bebbington, K. Proudfoot, and P. Jordan. 1994. Distinct intracellular localization of Lck and Fyn protein tyrosine kinases in human T-lymphocytes. J. Cell Biol. 125:639-649.
    • (1994) J. Cell Biol. , vol.125 , pp. 639-649
    • Ley, S.C.1    Marsh, M.2    Bebbington, C.R.3    Proudfoot, K.4    Jordan, P.5
  • 29
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis
    • Lisanti, M.P., P.E. Scherer, Z.L. Tang, and M. Sargiacomo. 1994. Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis, Trends Cell Biol. 4:231-235.
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.L.3    Sargiacomo, M.4
  • 30
    • 0027368868 scopus 로고
    • Analysis of the palmitoylation and membrane targeting domain of neuromodulin (GAP43) by site-specific mutagenesis
    • Liu, Y., D.A. Fisher, and D.R. Storm. 1993. Analysis of the palmitoylation and membrane targeting domain of neuromodulin (GAP43) by site-specific mutagenesis. Biochemistry. 32:10714-10719.
    • (1993) Biochemistry , vol.32 , pp. 10714-10719
    • Liu, Y.1    Fisher, D.A.2    Storm, D.R.3
  • 32
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLaughlin, S., and A. Aderem. 1995. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. TIBS. 20:272-276.
    • (1995) TIBS , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 33
    • 0019404632 scopus 로고
    • Two cellular proteins that immunoprecipitate with the transforming protein of Rous sarcoma virus
    • Oppermann, H., A.D. Levinson, L. Levintow, H.E. Varmus, J.M. Bishop, and S. Kawai. 1981. Two cellular proteins that immunoprecipitate with the transforming protein of Rous sarcoma virus. Virology. 113:736-751.
    • (1981) Virology , vol.113 , pp. 736-751
    • Oppermann, H.1    Levinson, A.D.2    Levintow, L.3    Varmus, H.E.4    Bishop, J.M.5    Kawai, S.6
  • 35
    • 0027222765 scopus 로고
    • A novel N-terminal motif for palmitoylation of G-prolein alpha subunits
    • Parenti, M., M.A. Vigano, C.M. Newman, G. Milligan, and A.I. Magee. 1993. A novel N-terminal motif for palmitoylation of G-prolein alpha subunits. Biochem. J. 291:349-353.
    • (1993) Biochem. J. , vol.291 , pp. 349-353
    • Parenti, M.1    Vigano, M.A.2    Newman, C.M.3    Milligan, G.4    Magee, A.I.5
  • 37
    • 0023441954 scopus 로고
    • Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor
    • Picard, D., and K. Yamamoto. 1987. Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO (Eur. Mol. Biol. Organ.) J. 6:3333-3340.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 3333-3340
    • Picard, D.1    Yamamoto, K.2
  • 38
    • 0028033931 scopus 로고
    • Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface
    • Quesnel, S., and J. R. Silvius. 1994. Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface. 'Biochemistry, 33:13340-13348.
    • (1994) Biochemistry , vol.33 , pp. 13340-13348
    • Quesnel, S.1    Silvius, J.R.2
  • 39
    • 0027772325 scopus 로고
    • Interaction of tyrosine kinase oncoproteins with cellular membranes
    • Resh, M.D. 1993. Interaction of tyrosine kinase oncoproteins with cellular membranes, Biochim. Biophys. Acta. 1155:307-322.
    • (1993) Biochim. Biophys. Acta. , vol.1155 , pp. 307-322
    • Resh, M.D.1
  • 40
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh, M.D. 1994. Myristylation and palmitylation of Src family members: the fats of the matter. Cell. 76:422-413.
    • (1994) Cell , vol.76 , pp. 422-1413
    • Resh, M.D.1
  • 41
    • 0030250003 scopus 로고    scopus 로고
    • Regulation of cellular signaling by fatty acid acylation and prenylation of signal transduction proteins
    • Resh M.D. 1996. Regulation of cellular signaling by fatty acid acylation and prenylation of signal transduction proteins. Cell Signaling. 8:403-112.
    • (1996) Cell Signaling , vol.8 , pp. 403-1112
    • Resh, M.D.1
  • 42
    • 0029014901 scopus 로고
    • Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae
    • Robbins S.M., N.A. Quintrell, and J.M. Bishop. 1995. Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae. Mol. Cell. Biol. 15:3507-3515.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3507-3515
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, J.M.3
  • 43
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl-phosphatidyiinositol-anchored protein targeting to a glycolipid-enriched membrane fraction
    • Rodgers W., B. Crise, and J.K. Rose. 1994. Signals determining protein tyrosine kinase and glycosyl-phosphatidyiinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Mol. Cell. Biol. 14:5384-5391.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5384-5391
    • Rodgers, W.1    Crise, B.2    Rose, J.K.3
  • 44
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman J.E., and L. Orci. 1992. Molecular dissection of the secretory pathway. Nature (Lond.). 355:409-415.
    • (1992) Nature (Lond.) , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 45
    • 0029767683 scopus 로고    scopus 로고
    • Lipid-modified, cysteinyl-containing peptides of diverse structures are efficiently S-acylated at the plasma membrane of mammalian cells
    • Shroeder, H., R. Leventis, S. Shahinian, P.A. Walton, and J.R. Silvius. 1996. Lipid-modified, cysteinyl-containing peptides of diverse structures are efficiently S-acylated at the plasma membrane of mammalian cells. J. Cell Biol. 134:647-660.
    • (1996) J. Cell Biol. , vol.134 , pp. 647-660
    • Shroeder, H.1    Leventis, R.2    Shahinian, S.3    Walton, P.A.4    Silvius, J.R.5
  • 46
    • 0028968896 scopus 로고
    • Douhly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes
    • Shahinian, S., and J. R. Silvius. 1995. Douhly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes. Biochemistry. 34:3813-3822.
    • (1995) Biochemistry , vol.34 , pp. 3813-3822
    • Shahinian, S.1    Silvius, J.R.2
  • 47
    • 0028175989 scopus 로고
    • Cysteine 3 of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A.M., D.J. Dietzen, J. Kwung, D.C. Link, and D.M. Lublin. 1994. Cysteine 3 of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae. J. Cell Biol. 126:353-363.
    • (1994) J. Cell Biol. , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwung, J.3    Link, D.C.4    Lublin, D.M.5
  • 49
    • 0028053759 scopus 로고
    • Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids
    • Sigal, C.T., W. Zhou, C.A. Buser,. S. McLaughlin, and M.D. Resh. 1994. Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids. Proc. Natl. Acad. Sci. USA. 91:12255-12257.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12255-12257
    • Sigal, C.T.1    Zhou, W.2    Buser, C.A.3    McLaughlin, S.4    Resh, M.D.5
  • 51
    • 0023940746 scopus 로고
    • The biology and enzymology of eukaryotic protein acylation
    • Towler, D.A., and J.I. Gordon. 1988. The biology and enzymology of eukaryotic protein acylation. Annu. Rev. Biochem. 57:69-99.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 69-99
    • Towler, D.A.1    Gordon, J.I.2
  • 52
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the ER membrane
    • Walter, P., and A.E. Johnson. 1994. Signal sequence recognition and protein targeting to the ER membrane. Annu. Rev. Cell Biol. 10:87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 53
    • 0030030373 scopus 로고    scopus 로고
    • Complementation between kinasedefective and activation-defectis'e TGF-β receptors reveals a novel form of receptor cooperaiivity essential for signaling
    • Weis-Garcia, F., and J. Massagué. 1996. Complementation between kinasedefective and activation-defectis'e TGF-β receptors reveals a novel form of receptor cooperaiivity essential for signaling. EMBO (Eur. Mol. Biol. Organ.) J. 15:276-289.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 276-289
    • Weis-Garcia, F.1    Massagué, J.2
  • 54
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilicox, C., J.-S. Hu, and E.N. Olson. 1987. Acylation of proteins with myristic acid occurs cotranslationally. Science (Wash. DC). 238:1275-1278.
    • (1987) Science (Wash. DC) , vol.238 , pp. 1275-1278
    • Wilcox, C.1    Hu, J.-S.2    Olson, E.N.3
  • 56
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F.L., and P.J. Casey. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65:241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 57
    • 0028218274 scopus 로고
    • Identification of a membrane binding domain within the amino terminal region of human immunodeficiency virus-1 Gag protein which interacts with acidic phospholipids
    • Zhou, W., L.J. Parent, J.W. Wills, and M.D. Resh. 1994. Identification of a membrane binding domain within the amino terminal region of human immunodeficiency virus-1 Gag protein which interacts with acidic phospholipids. J. Virol 68:2556-2569.
    • (1994) J. Virol , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4


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