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Volumn 6, Issue 4, 1996, Pages 432-438

Portrait of a myristoyl switch protein

Author keywords

[No Author keywords available]

Indexed keywords

RECOVERIN;

EID: 0030221268     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80106-0     Document Type: Article
Times cited : (122)

References (47)
  • 1
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilcox C, Hu J-S, Olson EN. Acylation of proteins with myristic acid occurs cotranslationally. Science. 238:1987;1275-1278.
    • (1987) Science , vol.238 , pp. 1275-1278
    • Wilcox, C.1    Hu J-S2    Olson, E.N.3
  • 5
    • 0025964349 scopus 로고
    • A 26 kd calcium binding protein from bovine rod outer segments as modulator of photoreceptor guanylate cyclase
    • Lambrecht HG, Koch KW. A 26 kd calcium binding protein from bovine rod outer segments as modulator of photoreceptor guanylate cyclase. EMBO J. 10:1991;793-798.
    • (1991) EMBO J , vol.10 , pp. 793-798
    • Lambrecht, H.G.1    Koch, K.W.2
  • 7
    • 0027419995 scopus 로고
    • The effect of recoverin-like calcium-binding proteins on the photoresponse of retinal rods
    • Gray-Keller MP, Polans AS, Palczewski K, Detwiler PB. The effect of recoverin-like calcium-binding proteins on the photoresponse of retinal rods. Neuron. 10:1993;523-531.
    • (1993) Neuron , vol.10 , pp. 523-531
    • Gray-Keller, M.P.1    Polans, A.S.2    Palczewski, K.3    Detwiler, P.B.4
  • 10
  • 12
    • 0026468238 scopus 로고
    • Calcium-myristoyl protein switch
    • Zozulya S, Stryer L. Calcium-myristoyl protein switch. Proc Natl Acad Sci USA. 89:1992;11569-11573.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11569-11573
    • Zozulya, S.1    Stryer, L.2
  • 15
    • 0028978240 scopus 로고
    • 2+-dependent interaction of recoverin with rhodopsin kinase
    • of special interest. Calcium-bound recoverin binds to rhodopsin kinase and inhibits the phosphorylation of light-excited rhodopsin.
    • 2+-dependent interaction of recoverin with rhodopsin kinase. J Biol Chem. 270:1995;18060-18066 Calcium-bound recoverin binds to rhodopsin kinase and inhibits the phosphorylation of light-excited rhodopsin.
    • (1995) J Biol Chem , vol.270 , pp. 18060-18066
    • Chen, C.K.1    Inglese, J.2    Lefkowitz, R.J.3    Hurley, J.B.4
  • 16
    • 0029033531 scopus 로고
    • Inhibition of rhodopsin kinase by recoverin
    • of special interest. Recoverin inhibition of rhodopsin kinase is observed in vitro at micromolar free calcium concentration which extrapolates to physiological calcium levels under the conditions of the intact rod cell.
    • of special interest Klenchin VA, Calvert PD, Bownds MD. Inhibition of rhodopsin kinase by recoverin. J Biol Chem. 270:1995;16147-16152 Recoverin inhibition of rhodopsin kinase is observed in vitro at micromolar free calcium concentration which extrapolates to physiological calcium levels under the conditions of the intact rod cell.
    • (1995) J Biol Chem , vol.270 , pp. 16147-16152
    • Klenchin, V.A.1    Calvert, P.D.2    Bownds, M.D.3
  • 17
    • 0028825379 scopus 로고
    • Rhodopsin kinase inhibition by recoverin: Function of recoverin myristoylation
    • Calvert PD, Klenchin VA, Bownds MD. Rhodopsin kinase inhibition by recoverin: function of recoverin myristoylation. J Biol Chem. 270:1995;24127-24129.
    • (1995) J Biol Chem , vol.270 , pp. 24127-24129
    • Calvert, P.D.1    Klenchin, V.A.2    Bownds, M.D.3
  • 18
    • 0028894334 scopus 로고
    • Calcium and membrane binding properties of bovine neurocalcin delta expressed in E. coli
    • 2+ to myristoylated, but not unmyristoylated, neurocalcin δ is shown to induce the binding of the protein to membranes.
    • 2+ to myristoylated, but not unmyristoylated, neurocalcin δ is shown to induce the binding of the protein to membranes.
    • (1995) J Biol Chem , vol.270 , pp. 3179-3185
    • Ladant, D.1
  • 19
    • 0027319966 scopus 로고
    • Molecular cloning of hippocalcin, a novel calcium-binding protein of the recoverin family
    • Kobayashi M, Takamatsu K, Saitoh S, Noguchi T. Molecular cloning of hippocalcin, a novel calcium-binding protein of the recoverin family. J Biol Chem. 268:1993;18898-18904.
    • (1993) J Biol Chem , vol.268 , pp. 18898-18904
    • Kobayashi, M.1    Takamatsu, K.2    Saitoh, S.3    Noguchi, T.4
  • 20
    • 0029874944 scopus 로고    scopus 로고
    • 2+-binding protein that associates with membranes and inhibits in vitro phosphorylation of bovine rhodopsin
    • 2+-binding protein that associates with membranes and inhibits in vitro phosphorylation of bovine rhodopsin. J Biol Chem. 271:1996;10256-10262.
    • (1996) J Biol Chem , vol.271 , pp. 10256-10262
    • Faurobert, E.1    Chen C-K2    Hurley, J.B.3    Teng, D.H.4
  • 21
    • 0030033414 scopus 로고    scopus 로고
    • Myristoylation-facilitated binding of the G protein ARF1 to membrane phospholipids is required for its activation by a soluble nucleotide exchange factor
    • of special interest. N-myristoylation of ARF promotes the exchange of GDP to GTP by facilitating the binding of ARF to phospholipid membranes.
    • of special interest Franco M, Chardin P, Chabre M, Paris S. Myristoylation-facilitated binding of the G protein ARF1 to membrane phospholipids is required for its activation by a soluble nucleotide exchange factor. J Biol Chem. 271:1996;1573-1578 N-myristoylation of ARF promotes the exchange of GDP to GTP by facilitating the binding of ARF to phospholipid membranes.
    • (1996) J Biol Chem , vol.271 , pp. 1573-1578
    • Franco, M.1    Chardin, P.2    Chabre, M.3    Paris, S.4
  • 22
    • 0029015710 scopus 로고
    • Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes
    • Moss J, Vaughan M. Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes. J Biol Chem. 270:1995;12327-12330.
    • (1995) J Biol Chem , vol.270 , pp. 12327-12330
    • Moss, J.1    Vaughan, M.2
  • 23
    • 0029007101 scopus 로고
    • The myristoylated amino terminus of ADP-ribosylation factor 1 is a phospholipid- and GTP-sensitive switch
    • Randazzo PA, Terui T, Sturch S, Fales HM, Ferrige AG, Kahn A. The myristoylated amino terminus of ADP-ribosylation factor 1 is a phospholipid- and GTP-sensitive switch. J Biol Chem. 270:1995;14809-14815.
    • (1995) J Biol Chem , vol.270 , pp. 14809-14815
    • Randazzo, P.A.1    Terui, T.2    Sturch, S.3    Fales, H.M.4    Ferrige, A.G.5    Kahn, A.6
  • 24
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini T, Orci L, Amherdt M, Brunner M, Kahn RA, Rothman JE. ADP-ribosylation factor is a subunit of the golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell. 67:1991;239-253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 25
    • 0024438997 scopus 로고
    • Myristoylated and nonmyristoylated forms of a protein are phosphorylated by protein kinase C
    • Graff JM, Gordon JI, Blackshear PJ. Myristoylated and nonmyristoylated forms of a protein are phosphorylated by protein kinase C. Science. 246:1989;503-506.
    • (1989) Science , vol.246 , pp. 503-506
    • Graff, J.M.1    Gordon, J.I.2    Blackshear, P.J.3
  • 26
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLauglin S, Aderem A. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem Sci. 20:1995;272-276.
    • (1995) Trends Biochem Sci , vol.20 , pp. 272-276
    • McLauglin, S.1    Aderem, A.2
  • 27
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh MD. Myristylation and palmitylation of Src family members: the fats of the matter. Cell. 76:1994;411-413.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 28
    • 0027429963 scopus 로고
    • Three-dimensional structure of recoverin, a calcium sensor in vision
    • Flaherty KM, Zozuiya S, Stryer L, McKay DB. Three-dimensional structure of recoverin, a calcium sensor in vision. Cell. 75:1993;709-716.
    • (1993) Cell , vol.75 , pp. 709-716
    • Flaherty, K.M.1    Zozuiya, S.2    Stryer, L.3    McKay, D.B.4
  • 30
    • 0028037860 scopus 로고
    • Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: Implications for the calcium-myristoyl switch
    • Ames JB, Tanaka T, Stryer L, Ikura M. Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch. Biochemistry. 33:1994;10743-10753.
    • (1994) Biochemistry , vol.33 , pp. 10743-10753
    • Ames, J.B.1    Tanaka, T.2    Stryer, L.3    Ikura, M.4
  • 31
    • 0029135419 scopus 로고
    • 2+-free state
    • 2+-free myristoylated recoverin obtained by NMR spectroscopy reveals that the myristoyl group is sequestered in a hydrophobic pocket formed by many aromatic residues from five flanking α helices.
    • 2+-free myristoylated recoverin obtained by NMR spectroscopy reveals that the myristoyl group is sequestered in a hydrophobic pocket formed by many aromatic residues from five flanking α helices.
    • (1995) Nature , vol.376 , pp. 444-447
    • Tanaka, T.1    Ames, J.B.2    Harvey, T.S.3    Stryer, L.4    Ikura, M.5
  • 32
    • 0029564421 scopus 로고
    • 2+-induced extrusion of the myristoyl group of recoverin
    • 2+ to recoverin induces the extrusion of its myristoyl group into solvent, which would enable it to interact with a lipid bilayer or hydrophobic site of a target protein.
    • 2+ to recoverin induces the extrusion of its myristoyl group into solvent, which would enable it to interact with a lipid bilayer or hydrophobic site of a target protein.
    • (1995) J Biol Chem , vol.270 , pp. 30909-30913
    • Ames, J.B.1    Tanaka, T.2    Ikura, M.3    Stryer, L.4
  • 33
    • 0029089024 scopus 로고
    • Calcium-dependent solvation of the myristoyl group of recoverin
    • of special interest. One-dimensional proton NMR spectra of calcium-bound recoverin indicate that the attached myristoyl group is solvent exposed.
    • of special interest Hughes RE, Brzovic PS, Klevit RE, Hurley JB. Calcium-dependent solvation of the myristoyl group of recoverin. Biochemistry. 34:1995;11410-11416 One-dimensional proton NMR spectra of calcium-bound recoverin indicate that the attached myristoyl group is solvent exposed.
    • (1995) Biochemistry , vol.34 , pp. 11410-11416
    • Hughes, R.E.1    Brzovic, P.S.2    Klevit, R.E.3    Hurley, J.B.4
  • 40
    • 0028152535 scopus 로고
    • Molecular characterization of human and mouse photoreceptor guanylate cyclase-activating protein (GCAP) and chromosomal localization of the human gene
    • Subbaraya I, Ruiz CC, Helekar BS, Zhao X, Gorczyca WA, Pettenati MJ, Rao PN, Palczewski K, Baehr W. Molecular characterization of human and mouse photoreceptor guanylate cyclase-activating protein (GCAP) and chromosomal localization of the human gene. J Biol Chem. 269:1994;31080-31089.
    • (1994) J Biol Chem , vol.269 , pp. 31080-31089
    • Subbaraya, I.1    Ruiz, C.C.2    Helekar, B.S.3    Zhao, X.4    Gorczyca, W.A.5    Pettenati, M.J.6    Rao, P.N.7    Palczewski, K.8    Baehr, W.9
  • 43
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly
    • Hill CP, Worthylake D, Bancroft DP, Christensen AM, Sundquist WI. Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc Natl Acad Sci USA. 93:1996;3099-3104.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 45
    • 0026244229 scopus 로고    scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures.
    • Kraulis P: MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis P1


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