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Volumn 314, Issue 18, 2008, Pages 3392-3404

Nuclear localization of Lyn tyrosine kinase mediated by inhibition of its kinase activity

Author keywords

Leptomycin B; Lipid modification; Lyn; Nuclear export; Nucleocytoplasmic transport; Src family tyrosine kinases; Tyrosine kinase activity

Indexed keywords

2,3 DIHYDRO 2 OXO 3 (4,5,6,7 TETRAHYDRO 1H INDOL 2 YLMETHYLENE) 1H INDOLE 5 SULFONIC ACID DIMETHYLAMIDE; LEPTOMYCIN B; PROTEIN KINASE LYN; PROTEIN TYROSINE KINASE;

EID: 56649121885     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.08.019     Document Type: Article
Times cited : (43)

References (51)
  • 3
    • 1042278767 scopus 로고    scopus 로고
    • Nuclear transport and cancer: from mechanism to intervention
    • Kau T.R., Way J.C., and Silver P.A. Nuclear transport and cancer: from mechanism to intervention. Nat. Rev. Cancer 4 (2004) 106-117
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 106-117
    • Kau, T.R.1    Way, J.C.2    Silver, P.A.3
  • 4
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown M.T., and Cooper J.A. Regulation, substrates and functions of src. Biochim. Biophys. Acta 1287 (1996) 121-149
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 5
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas S.M., and Brugge J.S. Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 13 (1997) 513-609
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 6
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P., and Hunter T. Oncogenic kinase signalling. Nature 411 (2001) 355-365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 7
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman T.J. A renaissance for SRC. Nat. Rev. Cancer 4 (2004) 470-480
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 9
    • 0032931978 scopus 로고    scopus 로고
    • Src-related protein tyrosine kinases in hematopoiesis
    • Corey S.J., and Anderson S.M. Src-related protein tyrosine kinases in hematopoiesis. Blood 93 (1999) 1-14
    • (1999) Blood , vol.93 , pp. 1-14
    • Corey, S.J.1    Anderson, S.M.2
  • 10
    • 0025913788 scopus 로고
    • Specific proto-oncogenic tyrosine kinases of Src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated
    • Tsukita S., Oishi K., Akiyama T., Yamanashi Y., Yamamoto T., and Tsukita S. Specific proto-oncogenic tyrosine kinases of Src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated. J. Cell Biol. 113 (1991) 867-879
    • (1991) J. Cell Biol. , vol.113 , pp. 867-879
    • Tsukita, S.1    Oishi, K.2    Akiyama, T.3    Yamanashi, Y.4    Yamamoto, T.5    Tsukita, S.6
  • 11
    • 0030997718 scopus 로고    scopus 로고
    • Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets
    • Hirao A., Hamaguchi I., Suda T., and Yamaguchi N. Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets. EMBO J. 16 (1997) 2342-2351
    • (1997) EMBO J. , vol.16 , pp. 2342-2351
    • Hirao, A.1    Hamaguchi, I.2    Suda, T.3    Yamaguchi, N.4
  • 12
    • 0032540356 scopus 로고    scopus 로고
    • Overexpression of C-terminal Src kinase homologous kinase suppresses activation of Lyn tyrosine kinase required for VLA5-mediated Dami cell spreading
    • Hirao A., Huang X.L., Suda T., and Yamaguchi N. Overexpression of C-terminal Src kinase homologous kinase suppresses activation of Lyn tyrosine kinase required for VLA5-mediated Dami cell spreading. J. Biol. Chem. 273 (1998) 10004-10010
    • (1998) J. Biol. Chem. , vol.273 , pp. 10004-10010
    • Hirao, A.1    Huang, X.L.2    Suda, T.3    Yamaguchi, N.4
  • 13
    • 0033531214 scopus 로고    scopus 로고
    • The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn
    • Hayashi T., Umemori H., Mishina M., and Yamamoto T. The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn. Nature 397 (1999) 72-76
    • (1999) Nature , vol.397 , pp. 72-76
    • Hayashi, T.1    Umemori, H.2    Mishina, M.3    Yamamoto, T.4
  • 14
    • 0033152305 scopus 로고    scopus 로고
    • A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucins CD34 and CD43 in immature hematopoietic cells
    • Tada J., Omine M., Suda T., and Yamaguchi N. A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucins CD34 and CD43 in immature hematopoietic cells. Blood 93 (1999) 3723-3735
    • (1999) Blood , vol.93 , pp. 3723-3735
    • Tada, J.1    Omine, M.2    Suda, T.3    Yamaguchi, N.4
  • 15
    • 0035020726 scopus 로고    scopus 로고
    • Overexpression of the Csk homologous kinase (Chk tyrosine kinase) induces multinucleation: a possible role for chromosome-associated Chk in chromosome dynamics
    • Yamaguchi N., Nakayama Y., Urakami T., Suzuki S., Nakamura T., Suda T., and Oku N. Overexpression of the Csk homologous kinase (Chk tyrosine kinase) induces multinucleation: a possible role for chromosome-associated Chk in chromosome dynamics. J. Cell Sci. 114 (2001) 1631-1641
    • (2001) J. Cell Sci. , vol.114 , pp. 1631-1641
    • Yamaguchi, N.1    Nakayama, Y.2    Urakami, T.3    Suzuki, S.4    Nakamura, T.5    Suda, T.6    Oku, N.7
  • 18
    • 2942640590 scopus 로고    scopus 로고
    • Trafficking of Lyn through the Golgi caveolin involves the charged residues on αE and αI helices in the kinase domain
    • Kasahara K., Nakayama Y., Ikeda K., Fukushima Y., Matsuda D., Horimoto S., and Yamaguchi N. Trafficking of Lyn through the Golgi caveolin involves the charged residues on αE and αI helices in the kinase domain. J. Cell Biol. 165 (2004) 641-652
    • (2004) J. Cell Biol. , vol.165 , pp. 641-652
    • Kasahara, K.1    Nakayama, Y.2    Ikeda, K.3    Fukushima, Y.4    Matsuda, D.5    Horimoto, S.6    Yamaguchi, N.7
  • 19
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: the fats of the matter
    • Resh M.D. Myristylation and palmitylation of Src family members: the fats of the matter. Cell 11 (1994) 411-413
    • (1994) Cell , vol.11 , pp. 411-413
    • Resh, M.D.1
  • 20
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451 (1999) 1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 22
    • 34250804789 scopus 로고    scopus 로고
    • Rapid trafficking of c-Src, a non-palmitoylated Src-family kinase, between the plasma membrane and late endosomes/lysosomes
    • Kasahara K., Nakayama Y., Kihara A., Matsuda D., Ikeda K., Kuga T., Fukumoto Y., Igarashi Y., and Yamaguchi N. Rapid trafficking of c-Src, a non-palmitoylated Src-family kinase, between the plasma membrane and late endosomes/lysosomes. Exp. Cell Res. 313 (2007) 2651-2666
    • (2007) Exp. Cell Res. , vol.313 , pp. 2651-2666
    • Kasahara, K.1    Nakayama, Y.2    Kihara, A.3    Matsuda, D.4    Ikeda, K.5    Kuga, T.6    Fukumoto, Y.7    Igarashi, Y.8    Yamaguchi, N.9
  • 23
    • 33645243620 scopus 로고    scopus 로고
    • Involvement of Golgi-associated Lyn tyrosine kinase in the translocation of annexin II to the endoplasmic reticulum under oxidative stress
    • Matsuda D., Nakayama Y., Horimoto S., Kuga T., Ikeda K., Kasahara K., and Yamaguchi N. Involvement of Golgi-associated Lyn tyrosine kinase in the translocation of annexin II to the endoplasmic reticulum under oxidative stress. Exp. Cell Res. 312 (2006) 1205-1217
    • (2006) Exp. Cell Res. , vol.312 , pp. 1205-1217
    • Matsuda, D.1    Nakayama, Y.2    Horimoto, S.3    Kuga, T.4    Ikeda, K.5    Kasahara, K.6    Yamaguchi, N.7
  • 25
    • 0029874049 scopus 로고    scopus 로고
    • Association of Lyn tyrosine kinase with the nuclear matrix and cell-cycle-dependent changes in matrix-associated tyrosine kinase activity
    • Radha V., Nambirajan S., and Swarup G. Association of Lyn tyrosine kinase with the nuclear matrix and cell-cycle-dependent changes in matrix-associated tyrosine kinase activity. Eur. J. Biochem. 236 (1996) 352-359
    • (1996) Eur. J. Biochem. , vol.236 , pp. 352-359
    • Radha, V.1    Nambirajan, S.2    Swarup, G.3
  • 26
    • 0033927555 scopus 로고    scopus 로고
    • Role for Lyn tyrosine kinase as a regulator of stress-activated protein kinase activity in response to DNA damage
    • Yoshida K., Weichselbaum R., Kharbanda S., and Kufe D. Role for Lyn tyrosine kinase as a regulator of stress-activated protein kinase activity in response to DNA damage. Mol. Cell. Biol. 20 (2000) 5370-5380
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5370-5380
    • Yoshida, K.1    Weichselbaum, R.2    Kharbanda, S.3    Kufe, D.4
  • 31
    • 14644433076 scopus 로고    scopus 로고
    • Multi-lobulation of the nucleus in prolonged S phase by nuclear expression of Chk tyrosine kinase
    • Nakayama Y., and Yamaguchi N. Multi-lobulation of the nucleus in prolonged S phase by nuclear expression of Chk tyrosine kinase. Exp. Cell Res. 304 (2005) 570-581
    • (2005) Exp. Cell Res. , vol.304 , pp. 570-581
    • Nakayama, Y.1    Yamaguchi, N.2
  • 32
    • 0029067675 scopus 로고
    • Golgi retention mechanism of β-1,4-galactosyltransferase: membrane-spanning domain-dependent homodimerization and association with α- and β-tubulins
    • Yamaguchi N., and Fukuda M.N. Golgi retention mechanism of β-1,4-galactosyltransferase: membrane-spanning domain-dependent homodimerization and association with α- and β-tubulins. J. Biol. Chem. 270 (1995) 12170-12176
    • (1995) J. Biol. Chem. , vol.270 , pp. 12170-12176
    • Yamaguchi, N.1    Fukuda, M.N.2
  • 33
    • 34247094761 scopus 로고    scopus 로고
    • Src signaling regulates completion of abscission in cytokinesis through ERK/MAPK activation at the midbody
    • Kasahara K., Nakayama Y., Nakazato Y., Ikeda K., Kuga T., and Yamaguchi N. Src signaling regulates completion of abscission in cytokinesis through ERK/MAPK activation at the midbody. J. Biol. Chem. 282 (2007) 5327-5339
    • (2007) J. Biol. Chem. , vol.282 , pp. 5327-5339
    • Kasahara, K.1    Nakayama, Y.2    Nakazato, Y.3    Ikeda, K.4    Kuga, T.5    Yamaguchi, N.6
  • 34
    • 0033060256 scopus 로고    scopus 로고
    • Induction of cell shape changes through activation of the interleukin-3 common β chain receptor by the RON receptor-type tyrosine kinase
    • Mera A., Suga M., Ando M., Suda T., and Yamaguchi N. Induction of cell shape changes through activation of the interleukin-3 common β chain receptor by the RON receptor-type tyrosine kinase. J. Biol. Chem. 274 (1999) 15766-15774
    • (1999) J. Biol. Chem. , vol.274 , pp. 15766-15774
    • Mera, A.1    Suga, M.2    Ando, M.3    Suda, T.4    Yamaguchi, N.5
  • 35
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilcox C., Hu J.S., and Olson E.N. 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.S.2    Olson, E.N.3
  • 36
    • 0021927037 scopus 로고
    • Myristic acid, a rare fatty acid, is the lipid attached to the transforming protein of Rous sarcoma virus and its cellular homolog
    • Buss J.E., and Sefton B.M. Myristic acid, a rare fatty acid, is the lipid attached to the transforming protein of Rous sarcoma virus and its cellular homolog. J. Virol. 53 (1985) 7-12
    • (1985) J. Virol. , vol.53 , pp. 7-12
    • Buss, J.E.1    Sefton, B.M.2
  • 37
    • 0035899499 scopus 로고    scopus 로고
    • Cleavage of Fyn and Lyn in their N-terminal unique regions during induction of apoptosis: a new mechanism for Src kinase regulation
    • Luciano F., Ricci J.E., and Auberger P. Cleavage of Fyn and Lyn in their N-terminal unique regions during induction of apoptosis: a new mechanism for Src kinase regulation. Oncogene 20 (2001) 4935-4941
    • (2001) Oncogene , vol.20 , pp. 4935-4941
    • Luciano, F.1    Ricci, J.E.2    Auberger, P.3
  • 38
    • 0035122485 scopus 로고    scopus 로고
    • Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase
    • Vigneri P., and Wang J.Y.J. Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase. Nat. Med. 7 (2001) 228-234
    • (2001) Nat. Med. , vol.7 , pp. 228-234
    • Vigneri, P.1    Wang, J.Y.J.2
  • 40
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle
    • Weis K. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112 (2003) 441-451
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 41
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M., Ohno M., Yoshida M., and Mattaj I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90 (1997) 1051-1060
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 42
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda M., Asano S., Nakamura T., Adachi M., Yoshida M., Yanagida M., and Nishida E. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390 (1997) 308-311
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 43
    • 33646268442 scopus 로고    scopus 로고
    • Nucleocytoplasmic trafficking of the Syk protein tyrosine kinase
    • Zhou F., Hu J., Ma H., Harrison M.L., and Geahlen R.L. Nucleocytoplasmic trafficking of the Syk protein tyrosine kinase. Mol. Cell. Biol. 26 (2006) 3478-3491
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3478-3491
    • Zhou, F.1    Hu, J.2    Ma, H.3    Harrison, M.L.4    Geahlen, R.L.5
  • 44
    • 0032077432 scopus 로고    scopus 로고
    • Insights into Src kinase functions: structural comparisons
    • Williams J.C., Wierenga R.K., and Saraste M. Insights into Src kinase functions: structural comparisons. Trends Biochem. Sci. 23 (1998) 179-184
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 179-184
    • Williams, J.C.1    Wierenga, R.K.2    Saraste, M.3
  • 45
    • 28444464082 scopus 로고    scopus 로고
    • The view from Awaji island: past, present, and future of RCC1 and the Ran GTPase system
    • Sazer S. The view from Awaji island: past, present, and future of RCC1 and the Ran GTPase system. Dev. Cell 9 (2005) 729-733
    • (2005) Dev. Cell , vol.9 , pp. 729-733
    • Sazer, S.1
  • 46
    • 0037389275 scopus 로고    scopus 로고
    • The p54 cleaved form of the tyrosine kinase Lyn generated by caspases during BCR-induced cell death in B lymphoma acts as a negative regulator of apoptosis
    • Luciano F., Herrant M., Jacquel A., Ricci J.E., and Auberger P. The p54 cleaved form of the tyrosine kinase Lyn generated by caspases during BCR-induced cell death in B lymphoma acts as a negative regulator of apoptosis. FASEB J. 17 (2003) 711-713
    • (2003) FASEB J. , vol.17 , pp. 711-713
    • Luciano, F.1    Herrant, M.2    Jacquel, A.3    Ricci, J.E.4    Auberger, P.5
  • 47
    • 0035964285 scopus 로고    scopus 로고
    • Interaction between growth arrest-DNA damage protein 34 and Src kinase Lyn negatively regulates genotoxic apoptosis
    • Grishin A.V., Azhipa O., Semenov I., and Corey S.J. Interaction between growth arrest-DNA damage protein 34 and Src kinase Lyn negatively regulates genotoxic apoptosis. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 10172-10177
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10172-10177
    • Grishin, A.V.1    Azhipa, O.2    Semenov, I.3    Corey, S.J.4
  • 51
    • 33846330967 scopus 로고    scopus 로고
    • Kip1 puzzle
    • Kip1 puzzle. Cell 128 (2007) 241-244
    • (2007) Cell , vol.128 , pp. 241-244
    • Kaldis, P.1


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