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Volumn 369, Issue 1, 2003, Pages 45-54

Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3ζ

Author keywords

Actin; Actin depolymerizing factor; Cytoskeletal dynamics; Testicular protein kinase 1 (TESK1)

Indexed keywords

PROTEINS; YEAST;

EID: 0037270323     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021152     Document Type: Article
Times cited : (73)

References (46)
  • 2
    • 0001954475 scopus 로고
    • Specific acidic proteins of the nervous system
    • Carlson, F. D., ed., Prentice-Hall, Englewood Cliffs, NJ
    • Moore, B. and Perez, V. J. (1967) Specific acidic proteins of the nervous system. In Physiological and Biochemical Aspects of Nervous Integration (Carlson, F. D., ed.), pp. 343-359, Prentice-Hall, Englewood Cliffs, NJ
    • (1967) Physiological and Biochemical Aspects of Nervous Integration , pp. 343-359
    • Moore, B.1    Perez, V.J.2
  • 3
    • 0030248429 scopus 로고    scopus 로고
    • 14-3-3 Proteins on the MAP
    • Aitken, A. (1996) 14-3-3 proteins on the MAP. Trends Cell Biol. 6, 341-347
    • (1996) Trends Cell Biol. , vol.6 , pp. 341-347
    • Aitken, A.1
  • 5
    • 0005312677 scopus 로고
    • Molecular cloning of cDNA coding for brain specific 14-3-3 protein, a protein kinase dependent activator of tyrosine and tryptophan hydroxylases
    • Ichimura, T., Isobe, T., Okuyama, T., Takahashi, N., Araki, K., Kuwano, R. and Takahashi, Y. (1988) Molecular cloning of cDNA coding for brain specific 14-3-3 protein, a protein kinase dependent activator of tyrosine and tryptophan hydroxylases. Proc. Natl. Acad. Sci. U.S.A. 85, 7084-7088
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7084-7088
    • Ichimura, T.1    Isobe, T.2    Okuyama, T.3    Takahashi, N.4    Araki, K.5    Kuwano, R.6    Takahashi, Y.7
  • 6
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and G2 checkpoint control: Regulation of 14-3-3 binding by phosphorylation of Cdc25C on Serine-2126
    • Peng, C. Y., Graves, P. R., Thomas, R. S., Wu, Z., Shaw, A. S. and Piwnica-Worms, H. (1997) Mitotic and G2 checkpoint control: regulation of 14-3-3 binding by phosphorylation of Cdc250 on Serine-2126. Science 277, 1501-1505
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.Y.1    Graves, P.R.2    Thomas, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 7
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha, J., Harda, H., Yang, E., Jockel, J. and Korsmeyer, S. J. (1996) Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87, 619-628
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harda, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 9
    • 0030999664 scopus 로고    scopus 로고
    • 14-3-3ε positively regulates Ras1 mediated signalling in Drosophila
    • Chang, H. C. and Rubin, G. M. (1997) 14-3-3ε positively regulates Ras1 mediated signalling in Drosophila. Genes Dev. 11, 1132-1139
    • (1997) Genes Dev. , vol.11 , pp. 1132-1139
    • Chang, H.C.1    Rubin, G.M.2
  • 10
    • 0031807577 scopus 로고    scopus 로고
    • 14-3-3 Proteins in neuronal development and function
    • Skoulakis, E. M. and Davis, R. L. (1998) 14-3-3 proteins in neuronal development and function. Mol. Neurobiol. 16, 269-284
    • (1998) Mol. Neurobiol. , vol.16 , pp. 269-284
    • Skoulakis, E.M.1    Davis, R.L.2
  • 11
    • 0026593018 scopus 로고
    • Exo1 and Exo2 proteins stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells
    • Morgan, A. and Burgoyne, D. (1992) Exo1 and Exo2 proteins stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. Nature (London) 355, 833-836
    • (1992) Nature (London) , vol.355 , pp. 833-836
    • Morgan, A.1    Burgoyne, D.2
  • 12
    • 0030822692 scopus 로고    scopus 로고
    • Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function
    • Broadie, K., Rushton, E., Skoulakis, E. M. and Davis, R. L. (1997) Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function. Neuron 19, 391-402
    • (1997) Neuron , vol.19 , pp. 391-402
    • Broadie, K.1    Rushton, E.2    Skoulakis, E.M.3    Davis, R.L.4
  • 14
    • 0028127003 scopus 로고
    • Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family
    • Reuther, G. W., Fu, H., Cripe, L. D., Collier, R. J. and Pendergast, A. M. (1994) Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family. Science 266, 129-133
    • (1994) Science , vol.266 , pp. 129-133
    • Reuther, G.W.1    Fu, H.2    Cripe, L.D.3    Collier, R.J.4    Pendergast, A.M.5
  • 15
    • 0029789477 scopus 로고    scopus 로고
    • Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 Overexpression results in inhibition of PKC theta translocation and function
    • Meller, N., Liu, Y. C., Collins, T. L., Bonnefoy-Berard, N., Baier, G., Isakov, N. and Altman, A. (1996) Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function. Mol. Cell. Biol. 16, 5782-5791
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5782-5791
    • Meller, N.1    Liu, Y.C.2    Collins, T.L.3    Bonnefoy-Berard, N.4    Baier, G.5    Isakov, N.6    Altman, A.7
  • 17
    • 0028032296 scopus 로고
    • 14-3-3 Modulators of signalling proteins?
    • Morrison, D. (1994) 14-3-3 modulators of signalling proteins? Science 266, 56-57
    • (1994) Science , vol.266 , pp. 56-57
    • Morrison, D.1
  • 18
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 polypeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • Rittinger, K., Budman, J., Xu, J., Volinia, S., Cantley, L. C., Smerdon, S. J., Gamblin, S. J. and Yaffe, M. B. (1999) Structural analysis of 14-3-3 polypeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol. Cell 4, 153-166
    • (1999) Mol. Cell , vol.4 , pp. 153-166
    • Rittinger, K.1    Budman, J.2    Xu, J.3    Volinia, S.4    Cantley, L.C.5    Smerdon, S.J.6    Gamblin, S.J.7    Yaffe, M.B.8
  • 19
    • 0028978947 scopus 로고
    • Distinct effects of a-SNAP, 14-3-3 proteins and calmodulin on priming and triggering of regulated exocytosis
    • Chamberlain, L. H., Roth, D., Morgan, A. and Burgoyne, R. D. (1995) Distinct effects of a-SNAP, 14-3-3 proteins and calmodulin on priming and triggering of regulated exocytosis. J. Cell Biol. 130, 1063-1070
    • (1995) J. Cell Biol. , vol.130 , pp. 1063-1070
    • Chamberlain, L.H.1    Roth, D.2    Morgan, A.3    Burgoyne, R.D.4
  • 20
    • 0028841609 scopus 로고
    • Stimulation of catecholamine secretion from adrenal chromaffin cells by 14-3-3 proteins is due to reorganization of the cortical actin network
    • Roth, D. and Burgoyne, R. D. (1995) Stimulation of catecholamine secretion from adrenal chromaffin cells by 14-3-3 proteins is due to reorganization of the cortical actin network. FEBS Lett. 374, 77-81
    • (1995) FEBS Lett. , vol.374 , pp. 77-81
    • Roth, D.1    Burgoyne, R.D.2
  • 21
    • 0032752399 scopus 로고    scopus 로고
    • Dominant negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae
    • Roth, D., Birkenfeld, J. and Betz, H. (1999) Dominant negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae. FEBS Lett. 460, 411-416
    • (1999) FEBS Lett. , vol.460 , pp. 411-416
    • Roth, D.1    Birkenfeld, J.2    Betz, H.3
  • 22
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg, J. R. (1999) Proteins of the ADF/cofilin family: Essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15, 185-230
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 23
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew, B. J., Minamide, L. S. and Bamburg, J. R. (1995) Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270, 17582-17587
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 24
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg, P. J., Ono, S., Minamide, L. S., Takahashi, M. and Bamburg, J. R. (1998) Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension. Cell Motil. Cytoskeleton 39, 172-190
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 25
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan, A. Y., Bailly, M., Zebda, N., Segall, J. E. and Condeelis, J. S. (2000) Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J. Cell Biol. 148, 531-542
    • (2000) J. Cell Biol. , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 30
    • 0029088586 scopus 로고
    • LIMK-1 and LIMK-2, two members of a LIM motif-containing protein kinase family
    • Nunoue, K., Ohashi, K., Okano, I. and Mizuno, K. (1995) LIMK-1 and LIMK-2, two members of a LIM motif-containing protein kinase family. Oncogene 11, 701-710
    • (1995) Oncogene , vol.11 , pp. 701-710
    • Nunoue, K.1    Ohashi, K.2    Okano, I.3    Mizuno, K.4
  • 31
    • 13344270389 scopus 로고
    • Identification and characterization of a novel protein kinase, TESK1, specifically expressed in testicular germ cells
    • Toshima, J., Ohashi, K., Okano, I., Nunoue, K., Kishioka, M., Kuma, K., Miyata, T., Hirai, M., Baba, T. and Mizuno, K. (1995) Identification and characterization of a novel protein kinase, TESK1, specifically expressed in testicular germ cells. J. Biol. Chem. 270, 31331-31337
    • (1995) J. Biol. Chem. , vol.270 , pp. 31331-31337
    • Toshima, J.1    Ohashi, K.2    Okano, I.3    Nunoue, K.4    Kishioka, M.5    Kuma, K.6    Miyata, T.7    Hirai, M.8    Baba, T.9    Mizuno, K.10
  • 32
    • 0035171699 scopus 로고    scopus 로고
    • Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation
    • Toshima, J., Toshima, J. Y., Amano, T., Yang, N., Narumiya, S. and Mizuno, K. (2001) Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. Mol. Biol. Cell 12, 1131-1145
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1131-1145
    • Toshima, J.1    Toshima, J.Y.2    Amano, T.3    Yang, N.4    Narumiya, S.5    Mizuno, K.6
  • 33
    • 0034602959 scopus 로고    scopus 로고
    • Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop
    • Ohashi, K., Nagata, K., Maekawa, M., Ishizaki, T., Narumiya, S. and Mizuno, K. (2000) Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. J. Biol. Chem. 275, 3577-3582
    • (2000) J. Biol. Chem. , vol.275 , pp. 3577-3582
    • Ohashi, K.1    Nagata, K.2    Maekawa, M.3    Ishizaki, T.4    Narumiya, S.5    Mizuno, K.6
  • 34
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards, D. C., Sanders, L. C., Bokoch, G. M. and Gill, G. N. (1999) Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell. Biol. 1, 253-258
    • (1999) Nat. Cell. Biol. , vol.1 , pp. 253-258
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 35
    • 0035933849 scopus 로고    scopus 로고
    • Activation of LIM-kinases by myotonic dystrophy kinase-related Cdc42-binding kinase α
    • Sumi, T., Matsumoto, K., Shibuya, A. and Nakamura, T. (2001) Activation of LIM-kinases by myotonic dystrophy kinase-related Cdc42-binding kinase α. J. Biol. Chem. 276, 23092-23096
    • (2001) J. Biol. Chem. , vol.276 , pp. 23092-23096
    • Sumi, T.1    Matsumoto, K.2    Shibuya, A.3    Nakamura, T.4
  • 36
    • 0027988403 scopus 로고
    • Kiz-1, a protein with LIM zinc fingers and kinase domains, is expressed mainly in neurons
    • Bernard, 0., Ganiatsas, S., Kannourakis, G. and Dringen, R. (1994) Kiz-1, a protein with LIM zinc fingers and kinase domains, is expressed mainly in neurons. Cell Growth Differ. 5, 1159-1171
    • (1994) Cell Growth Differ. , vol.5 , pp. 1159-1171
    • Bernard, O.1    Ganiatsas, S.2    Kannourakis, G.3    Dringen, R.4
  • 37
    • 0034887416 scopus 로고    scopus 로고
    • Inhibition of neurite extension by overexpression of individual domains of LIM kinase 1
    • Birkenfeld, J., Betz, H. and Roth, D. (2001) Inhibition of neurite extension by overexpression of individual domains of LIM kinase 1. J. Neurochem. 78, 924-927
    • (2001) J. Neurochem. , vol.78 , pp. 924-927
    • Birkenfeld, J.1    Betz, H.2    Roth, D.3
  • 38
    • 0028335641 scopus 로고
    • Molecular cloning of cDNAs for the zeta and theta subtypes of 14-3-3 protein and differential distribution of their mRNAs in the brain
    • Watanabe, M., Isobe, T., Ichimura, T., Kuwano, R., Takahashi, Y., Kondo, H. and Inoue, Y. (1994) Molecular cloning of cDNAs for the zeta and theta subtypes of 14-3-3 protein and differential distribution of their mRNAs in the brain. Mol. Brain Res. 25, 113-121
    • (1994) Mol. Brain Res. , vol.25 , pp. 113-121
    • Watanabe, M.1    Isobe, T.2    Ichimura, T.3    Kuwano, R.4    Takahashi, Y.5    Kondo, H.6    Inoue, Y.7
  • 39
    • 0003448569 scopus 로고
    • Cold Spring Harbour Laboratory Press, Cold Spring Harbor. NY
    • Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual, Cold Spring Harbour Laboratory Press, Cold Spring Harbor. NY
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 40
    • 0033574580 scopus 로고    scopus 로고
    • Structural features of Lim kinase that control effects on the actin cytoskeleton
    • Edwards, D. C. and Gill, G. N. (1999) Structural features of Lim kinase that control effects on the actin cytoskeleton. J. Biol. Chem. 274, 11352-11361
    • (1999) J. Biol. Chem. , vol.274 , pp. 11352-11361
    • Edwards, D.C.1    Gill, G.N.2
  • 41
    • 0034682667 scopus 로고    scopus 로고
    • 14-3-3ζ is an effector of tau protein phosphorylation
    • Hashiguchi, M., Sobue, K. and Paudel, H. K. (2000) 14-3-3ζ is an effector of tau protein phosphorylation. J. Biol. Chem. 275, 25247-25254
    • (2000) J. Biol. Chem. , vol.275 , pp. 25247-25254
    • Hashiguchi, M.1    Sobue, K.2    Paudel, H.K.3
  • 42
    • 0029947282 scopus 로고    scopus 로고
    • 14-3-3 Proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility factor
    • Liao, J. and Omary, M. B. (1996) 14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility factor. J. Cell Biol. 133, 345-357
    • (1996) J. Cell Biol. , vol.133 , pp. 345-357
    • Liao, J.1    Omary, M.B.2
  • 43
    • 0034703024 scopus 로고    scopus 로고
    • Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo
    • Tzivion, G., Luo, Z. J. and Avruch, J. (2000) Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo. J. Biol. Chem. 275, 29772-29778
    • (2000) J. Biol. Chem. , vol.275 , pp. 29772-29778
    • Tzivion, G.1    Luo, Z.J.2    Avruch, J.3
  • 44
    • 0035900680 scopus 로고    scopus 로고
    • Binding of 14-3-3 beta regulates the kinase activity and subcellular localization of testicular protein kinase 1
    • Toshima, J. Y., Toshima, J., Watanabe, T. and Mizuno, K. (2001) Binding of 14-3-3 beta regulates the kinase activity and subcellular localization of testicular protein kinase 1. J Biol Chem. 276, 43471-43461
    • (2001) J. Biol. Chem. , vol.276 , pp. 43471-43481
    • Toshima, J.Y.1    Toshima, J.2    Watanabe, T.3    Mizuno, K.4
  • 45
    • 0029829237 scopus 로고    scopus 로고
    • 14-3-3 Proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules
    • Vincenz, C. and Dixit, V. M. (1996) 14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules. J. Biol. Chem. 271, 20029-20034
    • (1996) J. Biol. Chem. , vol.271 , pp. 20029-20034
    • Vincenz, C.1    Dixit, V.M.2
  • 46
    • 0035798551 scopus 로고    scopus 로고
    • Identification of a novel interaction of 14-3-3 with pl90RhoGEF
    • Zhai, J., Lin, H., Shamim, M., Schlaepfer, W. W. and Canete-Soler, R. (2001) Identification of a novel interaction of 14-3-3 with pl90RhoGEF. J. Biol. Chem. 276, 41316-41324
    • (2001) J. Biol. Chem. , vol.276 , pp. 41316-41324
    • Zhai, J.1    Lin, H.2    Shamim, M.3    Schlaepfer, W.W.4    Canete-Soler, R.5


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