Involvement of the N-terminal unique domain of Chk tyrosine kinase in Chk-induced tyrosine phosphorylation in the nucleus

Experimental Cell Research

Volumn 312, Issue 12, 2006, Pages 2252-2263

  Nakayama, Yuji ^a   Kawana, Akiko ^a   Igarashi, Asae ^a   Yamaguchi, Naoto ^a  

^a CHIBA UNIVERSITY   (Japan)

Author keywords

Chk tyrosine kinase; Csk homologous kinase; Growth inhibition; Nuclear localization; Nuclear matrix; Src family kinase; Tyrosine phosphorylation

Indexed keywords

CHECKPOINT KINASE 1; PROTEIN TYROSINE KINASE; TRITON X 100;

AMINO TERMINAL SEQUENCE; ARTICLE; CELL NUCLEUS; CELL NUCLEUS MATRIX; CELL POPULATION; CELL PROLIFERATION; CHROMATIN; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; MITOSIS INHIBITION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN VARIANT; UPREGULATION;

EID: 33745226964     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2006.03.021     Document Type: Article

References (40)

1. Alonso A., Sasin J., Bottini N., Friedberg I., Friedberg I., Osterman A., Godzik A., Hunter T., Dixon J., and Mustelin T. Protein tyrosine phosphatases in the human genome. Cell 117 (2004) 699-711
2. Cans C., Mangano R., Barila D., Neubauer G., and Superti-Furga G. Nuclear tyrosine phosphorylation: the beginning of a map. Biochem. Pharmacol. 60 (2000) 1203-1215
3. Neet K., and Hunter T. Vertebrate non-receptor protein-tyrosine kinase families. Genes Cells 1 (1996) 147-169
4. Thomas S.M., and Brugge J.S. Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 13 (1997) 513-609
5. David-Pfeuty T., and Nouvian-Dooghe Y. Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells. J. Cell Biol. 111 (1990) 3097-3116
6. c-src with endosomal membranes in mammalian fibroblasts. J. Cell Biol. 118 (1992) 321-333
7. Ley S.C., Marsh M., Bebbington C.R., Proudfoot K., and Jordan P. Distinct intracellular localization of Lck and Fyn protein tyrosine kinases in human T lymphocytes. J. Cell Biol. 125 (1994) 639-649
8. 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
9. 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
10. Brown M.T., and Cooper J.A. Regulation, substrates and functions of Src. Biochim. Biophys. Acta 1287 (1996) 121-149
11. Cole P.A., Shen K., Qiao Y., and Wang D. Protein tyrosine kinases Src and Csk: a tail's tale. Curr. Opin. Chem. Biol. 7 (2003) 580-585
12. 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
13. 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
14. Nada S., Yagi T., Takeda H., Tokunaga T., Nakagawa H., Ikawa Y., Okada M., and Aizawa S. Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell 73 (1993) 1125-1135
15. Kawabuchi M., Satomi Y., Takao T., Shimonishi Y., Nada S., Nagai K., Tarakhovsky A., and Okada M. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Nature 404 (2000) 999-1003
16. Avraham H., and Price D.J. Regulation of megakaryocytopoiesis and platelet production by tyrosine kinases and tyrosine phosphatases. Methods 17 (1999) 250-264
17. Bougeret C., Jiang S., Keydar I., and Avraham H. Functional analysis of Csk and CHK kinases in breast cancer cells. J. Biol. Chem. 276 (2001) 33711-33720
18. Kim S., Zagozdzon R., Meisler A., Baleja J.D., Fu Y., Avraham S., and Avraham H. Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer. J. Biol. Chem. 277 (2002) 36465-36470
19. 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
20. Miyazaki J., Takaki S., Araki K., Tashiro F., Tominaga A., Takatsu K., and Yamamura K. Expression vector system based on the chicken β-actin promoter directs efficient production of interleukin-5. Gene 79 (1989) 269-277
21. c-Src. Nature 351 (1991) 69-72
22. 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
23. 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
24. 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
25. He D., Nickerson J.A., and Penman S. Core filaments of the nuclear matrix. J. Cell Biol. 110 (1990) 569-580
26. Takeuchi S., Takayama Y., Ogawa A., Tamura K., and Okada M. Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk. J. Biol. Chem. 275 (2000) 29183-29186
27. Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., and Avraham H. Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes. J. Biol. Chem. 272 (1997) 5915-5920
28. Zrihan-Licht S., Lim J., Keydar I., Sliwkowski M.X., Groopman J.E., and Avraham H. Association of Csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells. J. Biol. Chem. 272 (1997) 1856-1863
29. Zrihan-Licht S., Deng B., Yarden Y., McShan G., Keydar I., and Avraham H. Csk homologous kinase, a novel signaling molecule, directly associates with the activated ErbB-2 receptor in breast cancer cells and inhibits their proliferation. J. Biol. Chem. 273 (1998) 4065-4072
30. Yamashita H., Avraham S., Jiang S., Dikic I., and Avraham H. The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells. J. Biol. Chem. 274 (1999) 15059-15065
31. Chow L.M.L., Davidson D., Fournel M., Gosselin P., Lemieux S., Lyu M.S., Kozak C.A., Matis L.A., and Veillette A. Two distinct protein isoforms are encoded by ntk, a csk-related tyrosine protein kinase gene. Oncogene 9 (1994) 3437-3448
32. Lannutti B.J., and Drachman J.G. Lyn tyrosine kinase regulates thrombopoietin-induced proliferation of hematopoietic cell lines and primary megakaryocytic progenitors. Blood 103 (2004) 3736-3743
33. Lannutti B.J., Blake N., Gandhi M.J., Reems J.A., and Drachman J.G. Induction of polyploidization in leukemic cell lines and primary bone marrow by Src kinase inhibitor SU6656. Blood 105 (2005) 3875-3878
34. Tominaga T., Sahai E., Chardin P., McCormick F., Courtneidge S.A., and Alberts A.S. Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling. Mol. Cell 5 (2000) 13-25
35. Chong Y.P., Mulhern T.D., Zhu H.J., Fujita D.J., Bjorge J.D., Tantiongco J.P., Sotirellis N., Lio D.S.S., Scholz G., and Cheng H.C. A novel non-catalytic mechanism employed by the C-terminal Src-homologous kinase to inhibit Src-family kinase activity. J. Biol. Chem. 279 (2004) 20752-20766
36. Zagozdzon R., Kaminski R., Fu Y., Fu W., Bougeret C., and Avraham H.K. Csk homologous kinase (CHK), unlike Csk, enhances MAPK activation via Ras-mediated signaling in a Src-independent manner. Cell Signal 18 (2006) 871-881
37. Takayama Y., Tanaka S., Nagai K., and Okada M. Adenovirus-mediated overexpression of C-terminal Src kinase (Csk) in type I astrocytes interferes with cell spreading and attachment to fibronectin. J. Biol. Chem. 274 (1999) 2291-2297
38. Nickerson J.A. Experimental observations of a nuclear matrix. J. Cell Sci. 114 (2001) 463-474
39. Zink D., Fischer A.H., and Nickerson J.A. Nuclear structure in cancer cells. Nat. Rev., Cancer 4 (2004) 677-687
40. Mancini M.A., Shan B., Nickerson J.A., Penman S., and Lee W.-H. The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 418-422