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Volumn 57, Issue 2, 1999, Pages 256-267

A single human myosin light chain kinase gene (MLCK; MYLK) transcribes multiple nonmuscle isoforms

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN LIGHT CHAIN KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN);

EID: 0344758342     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.1999.5774     Document Type: Article
Times cited : (114)

References (48)
  • 1
    • 0028120416 scopus 로고
    • The biochemical basis of the regulation of smooth- muscle contraction
    • Allen B. G., Walsh M. P. The biochemical basis of the regulation of smooth- muscle contraction. Trends Biochem. Sci. 19:1994;362-368.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 362-368
    • Allen, B.G.1    Walsh, M.P.2
  • 3
    • 0026588409 scopus 로고
    • Astrocyte process growth induction by actin breakdown
    • Baorto D. M., Mellado W., Shelanski M. L. Astrocyte process growth induction by actin breakdown. J. Cell Biol. 117:1992;357-367.
    • (1992) J. Cell Biol. , vol.117 , pp. 357-367
    • Baorto, D.M.1    Mellado, W.2    Shelanski, M.L.3
  • 4
    • 0031904240 scopus 로고    scopus 로고
    • Organization of the genetic locus for chicken myosin light chain kinase is complex: Multiple proteins are encoded and exhibit differential expression and localization
    • Birukov K. G., Schavocky J. P., Shirinsky V. P., Chibalina M. V., Van Eldik L. J., Watterson D. W. Organization of the genetic locus for chicken myosin light chain kinase is complex: Multiple proteins are encoded and exhibit differential expression and localization. J. Cell. Biochem. 70:1998;402-413.
    • (1998) J. Cell. Biochem. , vol.70 , pp. 402-413
    • Birukov, K.G.1    Schavocky, J.P.2    Shirinsky, V.P.3    Chibalina, M.V.4    Van Eldik, L.J.5    Watterson, D.W.6
  • 6
    • 0021200684 scopus 로고
    • Evidence for a role of myosin phosphorylation in the initiation of the platelet shape change response
    • Daniel J. L., Molish I. R., Rigmaiden M., Stewart G. Evidence for a role of myosin phosphorylation in the initiation of the platelet shape change response. J. Biol. Chem. 259:1984;9826-9831.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9826-9831
    • Daniel, J.L.1    Molish, I.R.2    Rigmaiden, M.3    Stewart, G.4
  • 7
    • 0029620472 scopus 로고
    • Developmental and tissue distribution of expression of non muscle and smooth muscle isoforms of myosin light chain kinase
    • Fisher S. A., Ikebe M. Developmental and tissue distribution of expression of non muscle and smooth muscle isoforms of myosin light chain kinase. Biochem. Biophys. Res. Commun. 217:1995;696-703.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 696-703
    • Fisher, S.A.1    Ikebe, M.2
  • 8
    • 0025837663 scopus 로고
    • Microinjection of the catalytic fragment of myosin light chain kinase into dividing cells: Effects on mitosis and cytokinesis
    • Fishkind D. J., Cao L., Wang Y. Microinjection of the catalytic fragment of myosin light chain kinase into dividing cells: Effects on mitosis and cytokinesis. J. Cell Biol. 114:1991;967-975.
    • (1991) J. Cell Biol. , vol.114 , pp. 967-975
    • Fishkind, D.J.1    Cao, L.2    Wang, Y.3
  • 9
    • 0026343743 scopus 로고
    • The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin
    • Gallagher P. J., Herring P. B. The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin. J. Biol. Chem. 266:1991;23945-23952.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23945-23952
    • Gallagher, P.J.1    Herring, P.B.2
  • 10
    • 0026340753 scopus 로고
    • Molecular characterization of a mammalian smooth muscle myosin light chain kinase
    • Gallagher P. J., Herring P. B., Griffin S. A., Stull J. T. Molecular characterization of a mammalian smooth muscle myosin light chain kinase. J. Biol. Chem. 266:1991;23936-23944.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23936-23944
    • Gallagher, P.J.1    Herring, P.B.2    Griffin, S.A.3    Stull, J.T.4
  • 11
    • 0028788167 scopus 로고
    • Expression of a novel myosin light chain kinase in embryonic tissues and cultured cells
    • Gallagher P. J., Garcia J. G. N., Herring P. B. Expression of a novel myosin light chain kinase in embryonic tissues and cultured cells. J. Biol. Chem. 270:1995;29090-29095.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29090-29095
    • Gallagher, P.J.1    Garcia, J.G.N.2    Herring, P.B.3
  • 12
    • 0029012398 scopus 로고
    • Regulation of endothelial cell myosin light chain phosphorylation: Role in thrombin-induced barrier dysfunction
    • Garcia J. G. N., Davis H. W., Patterson C. E. Regulation of endothelial cell myosin light chain phosphorylation: Role in thrombin-induced barrier dysfunction. J. Cell. Physiol. 163:1995;510-522.
    • (1995) J. Cell. Physiol. , vol.163 , pp. 510-522
    • Garcia, J.G.N.1    Davis, H.W.2    Patterson, C.E.3
  • 16
    • 0032127329 scopus 로고    scopus 로고
    • Regulation of endothelial cell myosin light chain phosphorylation and permeability by vanadate
    • Gilbert-McClain L. I., Verin A. D., Shi S., Irwin R. P., Garcia J. G. N. Regulation of endothelial cell myosin light chain phosphorylation and permeability by vanadate. J. Cell. Biochem. 70:1998;141-155.
    • (1998) J. Cell. Biochem. , vol.70 , pp. 141-155
    • Gilbert-McClain, L.I.1    Verin, A.D.2    Shi, S.3    Irwin, R.P.4    Garcia, J.G.N.5
  • 17
    • 0029119895 scopus 로고
    • Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isometric tension, actin polymerization, and myosin phosphorylation
    • Goeckeler Z. M., Wysolmerski R. B. Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isometric tension, actin polymerization, and myosin phosphorylation. J. Cell Biol. 130:1995;622-635.
    • (1995) J. Cell Biol. , vol.130 , pp. 622-635
    • Goeckeler, Z.M.1    Wysolmerski, R.B.2
  • 18
    • 0022869168 scopus 로고
    • Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA
    • Guerriero V. Jr., Russo M. A., Olson N. J., Putkey J. A., Means A. R. Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA. Biochemistry. 25:1986;8372-8381.
    • (1986) Biochemistry , vol.25 , pp. 8372-8381
    • Guerriero V., Jr.1    Russo, M.A.2    Olson, N.J.3    Putkey, J.A.4    Means, A.R.5
  • 19
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new set which is close to that containing variable domains
    • Harpaz Y., Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new set which is close to that containing variable domains. J. Mol. Biol. 13:1994;528-539.
    • (1994) J. Mol. Biol. , vol.13 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 20
    • 0023041527 scopus 로고
    • The growing immunoglobulin gene family
    • Hunkapiller T., Hood L. The growing immunoglobulin gene family. Nature (London). 323:1986;15-16.
    • (1986) Nature (London) , vol.323 , pp. 15-16
    • Hunkapiller, T.1    Hood, L.2
  • 21
    • 0024330080 scopus 로고
    • Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase
    • Ito M., Dabrowska R., Guerriero V., Hartshorne D. J. Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase. J. Biol. Chem. 264:1989;13971-13974.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13971-13974
    • Ito, M.1    Dabrowska, R.2    Guerriero, V.3    Hartshorne, D.J.4
  • 23
    • 0026582867 scopus 로고
    • Toward a molecular understanding of titin
    • Labeit S., Gautel M., Lakey A., Trinick J. Toward a molecular understanding of titin. EMBO J. 11:1992;1711-1716.
    • (1992) EMBO J. , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 24
    • 0023695794 scopus 로고
    • Regulation of actin microfilament integrity in living nonmuscle cells by cAMP-dependent protein kinase and the myosin light chain kinase
    • Lamb N. J. C., Fermandez A., Conti M. A. Regulation of actin microfilament integrity in living nonmuscle cells by cAMP-dependent protein kinase and the myosin light chain kinase. J. Cell Biol. 106:1988;1955-1971.
    • (1988) J. Cell Biol. , vol.106 , pp. 1955-1971
    • Lamb, N.J.C.1    Fermandez, A.2    Conti, M.A.3
  • 26
    • 0025185134 scopus 로고
    • Effect of inhibitors of myosin light chain kinase and other protein kinases on the first cell division of sea urchin eggs
    • Mabuchi I., Takano-Ohmuro H. Effect of inhibitors of myosin light chain kinase and other protein kinases on the first cell division of sea urchin eggs. Dev. Growth Differ. 32:1990;549-556.
    • (1990) Dev. Growth Differ. , vol.32 , pp. 549-556
    • Mabuchi, I.1    Takano-Ohmuro, H.2
  • 27
    • 0032498625 scopus 로고    scopus 로고
    • Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation
    • Mills J. C., Stone N. L., Erhardt J., Pittman R. N. Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation. J. Cell Biol. 140:1998;627-636.
    • (1998) J. Cell Biol. , vol.140 , pp. 627-636
    • Mills, J.C.1    Stone, N.L.2    Erhardt, J.3    Pittman, R.N.4
  • 28
    • 0344708671 scopus 로고
    • Myosin may be involved in the neurotransmitter release mechanism at the synapse formed between rat sympathetic neurons in culture
    • Mochida S., Nonomura Y., Kobayashi H., Libet B. Myosin may be involved in the neurotransmitter release mechanism at the synapse formed between rat sympathetic neurons in culture. Soc. Neurosci. Abstr. 19:1993;384.
    • (1993) Soc. Neurosci. Abstr. , vol.19 , pp. 384
    • Mochida, S.1    Nonomura, Y.2    Kobayashi, H.3    Libet, B.4
  • 29
    • 0027983926 scopus 로고
    • Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture
    • Mochida S., Kobayashi H., Matsuda Y., Yuda Y., Muramato K., Nonomura Y. Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture. Neuron. 13:1994;1131-1142.
    • (1994) Neuron , vol.13 , pp. 1131-1142
    • Mochida, S.1    Kobayashi, H.2    Matsuda, Y.3    Yuda, Y.4    Muramato, K.5    Nonomura, Y.6
  • 30
    • 0020050314 scopus 로고
    • A catalogue of splice junction sequences
    • Mount S. M. A catalogue of splice junction sequences. Nucleic Acids Res. 10:1982;459-472.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 459-472
    • Mount, S.M.1
  • 32
    • 0027986575 scopus 로고
    • Mechanisms of cholera toxin prevention of thrombin- And PMA-induced endothelial cell barrier dysfunction
    • Patterson C. E., Davis H., Schaphorst K., Garcia J. G. N. Mechanisms of cholera toxin prevention of thrombin- and PMA-induced endothelial cell barrier dysfunction. Microvasc. Res. 48:1994;212-235.
    • (1994) Microvasc. Res. , vol.48 , pp. 212-235
    • Patterson, C.E.1    Davis, H.2    Schaphorst, K.3    Garcia, J.G.N.4
  • 33
    • 0028825693 scopus 로고
    • The human myosin light chain kinase (MLCK) from hippocampus: Cloning, sequencing, expression, and localization to 3qcen-q21
    • Potier M.-C., Chelot E., Pekarsky Y., Gardiner K., Rossier J., Turnell W. G. The human myosin light chain kinase (MLCK) from hippocampus: Cloning, sequencing, expression, and localization to 3qcen-q21. Genomics. 29:1995;562-570.
    • (1995) Genomics , vol.29 , pp. 562-570
    • Potier, M.-C.1    Chelot, E.2    Pekarsky, Y.3    Gardiner, K.4    Rossier, J.5    Turnell, W.G.6
  • 34
    • 0028863479 scopus 로고
    • Psgl-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus
    • Pouyani T., Seed B. Psgl-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. Cell. 83:1995;333-343.
    • (1995) Cell , vol.83 , pp. 333-343
    • Pouyani, T.1    Seed, B.2
  • 36
    • 0027439594 scopus 로고
    • Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125 FAK
    • Schaller M. D., Borgman C. A., Parson J. T. Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125 FAK. Mol. Cell. Biol. 13:1993;785-791.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 785-791
    • Schaller, M.D.1    Borgman, C.A.2    Parson, J.T.3
  • 37
    • 0032240960 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in thrombin-induced endothelial cell contraction and barrier dysfunction
    • Shi S., Verin A. D., Gilbert-McClain L. I., Schaphorst K. L., Irwin R., Garcia J. G. N. Role of tyrosine phosphorylation in thrombin-induced endothelial cell contraction and barrier dysfunction. Endothelium. 6:1998;153-171.
    • (1998) Endothelium , vol.6 , pp. 153-171
    • Shi, S.1    Verin, A.D.2    Gilbert-McClain, L.I.3    Schaphorst, K.L.4    Irwin, R.5    Garcia, J.G.N.6
  • 39
    • 0025148992 scopus 로고
    • Use of DNA sequence and mutant analysis and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity
    • Shoemaker M. O., Lau W., Shattuck R. L., Kwiatkowski A. P., Matrisian P. E., Guerra-Santos L., Wilson E., Lukas T. J., Van Eldik L. J., Watterson D. M. Use of DNA sequence and mutant analysis and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity. J. Cell Biol. 111:1990;1107-1125.
    • (1990) J. Cell Biol. , vol.111 , pp. 1107-1125
    • Shoemaker, M.O.1    Lau, W.2    Shattuck, R.L.3    Kwiatkowski, A.P.4    Matrisian, P.E.5    Guerra-Santos, L.6    Wilson, E.7    Lukas, T.J.8    Van Eldik, L.J.9    Watterson, D.M.10
  • 44
    • 0020318329 scopus 로고
    • Neuronal cell Thy-1 glycoprotein-homology with immunoglobulin
    • Williams A. F., Gagnon J. Neuronal cell Thy-1 glycoprotein-homology with immunoglobulin. Science. 216:1982;696-703.
    • (1982) Science , vol.216 , pp. 696-703
    • Williams, A.F.1    Gagnon, J.2
  • 45
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily-domains for surface recognition
    • Williams A. F., Barclay A. N. The immunoglobulin superfamily-domains for surface recognition. Annu. Rev. Immunol. 6:1988;381-405.
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 46
    • 0025186832 scopus 로고
    • Involvement of myosin light chain kinase in endothelial cell retraction
    • Wysolmerski R. B., Lagunoff D. Involvement of myosin light chain kinase in endothelial cell retraction. Proc. Natl. Acad. Sci. USA. 87:1990;16-20.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 16-20
    • Wysolmerski, R.B.1    Lagunoff, D.2
  • 47
    • 0028123676 scopus 로고
    • In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells
    • Yamakita Y., Yamashiro S., Matsumura F. In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells. J. Cell. Biol. 124:1994;129-137.
    • (1994) J. Cell. Biol. , vol.124 , pp. 129-137
    • Yamakita, Y.1    Yamashiro, S.2    Matsumura, F.3
  • 48
    • 0027096576 scopus 로고
    • Molecular cloning of the chicken gizzard telokin gene and cDNA
    • Yoshikai S., Ikebe M. Molecular cloning of the chicken gizzard telokin gene and cDNA. Arch. Biochem. Biophys. 299:1992;242-247.
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 242-247
    • Yoshikai, S.1    Ikebe, M.2


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