메뉴 건너뛰기




Volumn 29, Issue 5, 1996, Pages 543-552

The synaptic protein UNC-18 is phosphorylated by protein kinase C

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; NERVE PROTEIN; PROTEIN KINASE C; SERINE; THREONINE;

EID: 0030296517     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/0197-0186(96)00009-5     Document Type: Article
Times cited : (15)

References (28)
  • 1
    • 0023741304 scopus 로고
    • An improved purification procedure and properties of casein kinase II from brain
    • Alcázar A., Martin E., Fando J. L. and Salinas M. (1988) An improved purification procedure and properties of casein kinase II from brain. Neurochem. Res. 13, 829-836.
    • (1988) Neurochem. Res. , vol.13 , pp. 829-836
    • Alcázar, A.1    Martin, E.2    Fando, J.L.3    Salinas, M.4
  • 2
    • 0028342804 scopus 로고
    • Regulated vesicular fusion in neurons: Snapping together the details
    • Bark I. C. and Wilson M. C. (1994) Regulated vesicular fusion in neurons: snapping together the details. Proc. Natl Acad. Sci. U.S.A. 91, 4621-4624.
    • (1994) Proc. Natl Acad. Sci. U.S.A. , vol.91 , pp. 4621-4624
    • Bark, I.C.1    Wilson, M.C.2
  • 4
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett M. K. and Scheller R. H. (1993) The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl Acad. Sci. U.S.A. 90, 2559-2563.
    • (1993) Proc. Natl Acad. Sci. U.S.A. , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 5
    • 0025998840 scopus 로고
    • Phosphopeptide mapping phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle W. J., van der Geer P. and Hunter T. (1991) Phosphopeptide mapping phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Meths Enzymol. 201, 110-149.
    • (1991) Meths Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 6
    • 0025309605 scopus 로고
    • Pathways to regulated exocytosis in neurons
    • De Camilli P. and Jahn R. (1990) Pathways to regulated exocytosis in neurons. Ann. Rev. Physiol. 52, 625-645.
    • (1990) Ann. Rev. Physiol. , vol.52 , pp. 625-645
    • De Camilli, P.1    Jahn, R.2
  • 9
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P., Voltorta F., Czernik A. J. and Benfenati F. (1993) Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259, 780-785.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Voltorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 10
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata Y., Slaughter C. A. and Südhof T. C. (1993) Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366, 347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Südhof, T.C.3
  • 11
    • 0026582816 scopus 로고
    • The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans
    • Hosono R., Hekimi S., Kamiya Y., Sassa T., Murakami S., Nishiwaki S., Miwa J., Taketo A. and Kodaira K. (1992) The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans. J. Neurochem. 58, 1517-1525.
    • (1992) J. Neurochem. , vol.58 , pp. 1517-1525
    • Hosono, R.1    Hekimi, S.2    Kamiya, Y.3    Sassa, T.4    Murakami, S.5    Nishiwaki, S.6    Miwa, J.7    Taketo, A.8    Kodaira, K.9
  • 12
    • 0023616451 scopus 로고
    • Mutations affecting acetylcholine levels in the nematode Caenorhabditis elegans
    • Hosono R., Sassa T. and Kuno S. (1987) Mutations affecting acetylcholine levels in the nematode Caenorhabditis elegans. J. Neurochem. 49, 1820-1823.
    • (1987) J. Neurochem. , vol.49 , pp. 1820-1823
    • Hosono, R.1    Sassa, T.2    Kuno, S.3
  • 13
    • 0001114327 scopus 로고
    • Spontaneous mutations of trichlorfon resistance in the nematode Caenorhabditis elegans
    • Hosono R., Sassa T. and Kuno S. (1989) Spontaneous mutations of trichlorfon resistance in the nematode Caenorhabditis elegans. Zool. Sci. 6, 697-708.
    • (1989) Zool. Sci. , vol.6 , pp. 697-708
    • Hosono, R.1    Sassa, T.2    Kuno, S.3
  • 14
    • 0019327140 scopus 로고
    • Phosphorylation of calf thymus H1 histone by calcium-activated, phospholipid-dependent protein kinase
    • Iwasa Y., Takai Y., Kikkawa U. and Nishizuka Y. (1980) Phosphorylation of calf thymus H1 histone by calcium-activated, phospholipid-dependent protein kinase. Biochem. Biophys. Res. Commun. 96, 180-187.
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 180-187
    • Iwasa, Y.1    Takai, Y.2    Kikkawa, U.3    Nishizuka, Y.4
  • 15
    • 0027263007 scopus 로고
    • Synaptic vesicle traffic: Rush hour in the nerve terminal
    • Jahn R. and Südhof T. C. (1993) Synaptic vesicle traffic: rush hour in the nerve terminal. J. Neurochem. 61, 12-21.
    • (1993) J. Neurochem. , vol.61 , pp. 12-21
    • Jahn, R.1    Südhof, T.C.2
  • 16
    • 0027419032 scopus 로고
    • Storage and release of neurotransmitters
    • Review supplement to Cell 72
    • Kelly R. B. (1993) Storage and release of neurotransmitters. Review supplement to Cell 72, Neuron 10, 45-53.
    • (1993) Neuron , vol.10 , pp. 45-53
    • Kelly, R.B.1
  • 17
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence motifs
    • Kemp B. E. and Pearson R. B. (1990) Protein kinase recognition sequence motifs. Trends Biochem. Sci. 15, 342-346.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 18
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatase
    • 558
    • Kennelly P. J. and Krebs E. G. (1991) Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatase. J. Biol. Chem. 266, 15,555-15,558.
    • (1991) J. Biol. Chem. , vol.266 , Issue.15 , pp. 555-515
    • Kennelly, P.J.1    Krebs, E.G.2
  • 19
    • 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 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0028240128 scopus 로고
    • Structure and expression of a novel, neuronal protein kinase C (PKC1B) from Caenorhabditis elegans
    • Land M., Islas-Trejo A., Freedman J. H. and Rubin C. S. (1994) Structure and expression of a novel, neuronal protein kinase C (PKC1B) from Caenorhabditis elegans. J. Biol. Chem. 269, 9234-9244.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9234-9244
    • Land, M.1    Islas-Trejo, A.2    Freedman, J.H.3    Rubin, C.S.4
  • 21
    • 0030297090 scopus 로고    scopus 로고
    • Expression, purification and characterization of recombinant C. elegans UNC-18
    • Ogawa H., Hayashi N., Hori I., Kobayashi T. and Hosono R. (1996) Expression, purification and characterization of recombinant C. elegans UNC-18. Neurochem. Int. 29, 563-573.
    • (1996) Neurochem. Int. , vol.29 , pp. 563-573
    • Ogawa, H.1    Hayashi, N.2    Hori, I.3    Kobayashi, T.4    Hosono, R.5
  • 23
    • 0020972355 scopus 로고
    • Assay of protein kinase
    • Roskoski Jr. R. (1983) Assay of protein kinase. Meths Enzymol. 99, 3-6.
    • (1983) Meths Enzymol. , vol.99 , pp. 3-6
    • Roskoski R., Jr.1
  • 24
    • 0027315483 scopus 로고
    • The Drosophila Ras2 and Rop gene pair: A dual homology with a yeast Ras-like gene and a suppresor of its loss-of-function phenotype
    • Salzberg A., Cohen N., Halachmi N., Kimchie Z. and Lev Z. (1993) The Drosophila Ras2 and Rop gene pair: a dual homology with a yeast Ras-like gene and a suppresor of its loss-of-function phenotype. Development 117, 1309-1319.
    • (1993) Development , vol.117 , pp. 1309-1319
    • Salzberg, A.1    Cohen, N.2    Halachmi, N.3    Kimchie, Z.4    Lev, Z.5
  • 25
    • 0026543890 scopus 로고
    • Purification and characterization of protein kinase C from the nematode Caenorhabditis elegans
    • Sassa T. and Miwa J. (1992) Purification and characterization of protein kinase C from the nematode Caenorhabditis elegans. Biochem. J. 282, 219-223.
    • (1992) Biochem. J. , vol.282 , pp. 219-223
    • Sassa, T.1    Miwa, J.2
  • 26
    • 0025797676 scopus 로고
    • A manual sequencing method for identification of phosphorylated amino acids in phosphopeptides
    • Sullivan S. and Wong T. W. (1991) A manual sequencing method for identification of phosphorylated amino acids in phosphopeptides. Analyt. Biochem. 197, 65-68.
    • (1991) Analyt. Biochem. , vol.197 , pp. 65-68
    • Sullivan, S.1    Wong, T.W.2
  • 27
    • 0024981819 scopus 로고
    • Mutations in a protein kinase C homolog confer phorbol ester resistance on Caenorhabditis elegans
    • Tabuse Y., Nishiwaki K. and Miwa J. (1989) Mutations in a protein kinase C homolog confer phorbol ester resistance on Caenorhabditis elegans. Science 243, 1713-1716.
    • (1989) Science , vol.243 , pp. 1713-1716
    • Tabuse, Y.1    Nishiwaki, K.2    Miwa, J.3
  • 28
    • 0021751717 scopus 로고
    • Affinity chromatography of protein kinase C-phorbol ester receptor on polyacrylamide-immobilized phosphatidylserine
    • 314
    • Uchida T. and Filburn C. R. (1984) Affinity chromatography of protein kinase C-phorbol ester receptor on polyacrylamide-immobilized phosphatidylserine. J. Biol. Chem. 259, 12,311-12,314.
    • (1984) J. Biol. Chem. , vol.259 , Issue.12 , pp. 311-312
    • Uchida, T.1    Filburn, C.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.