HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hirao, A. Articles by Yamaguchi, N. Search for Related Content PubMed PubMed Citation Articles by Hirao, A. Articles by Yamaguchi, N. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 16, 10004-10010, April 17, 1998

Overexpression of C-terminal Src Kinase Homologous Kinase Suppresses Activation of Lyn Tyrosine Kinase Required for VLA5-mediated Dami Cell Spreading

From the Department of Cell Differentiation, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto 860-0811, Japan

The Csk homologous kinase (Chk), which is co-expressed with C-terminal Src kinase (Csk) in hematopoietic cells, negatively regulates Src family kinases in vitro with selectivity toward Lyn but not c-Src in platelets. To explore the role of Src family kinases in hematopoietic cell adhesion, we overexpressed Chk in the megakaryocytic cell line Dami and established clones exhibiting a 10-fold increase in the amount of Chk. Overexpression of Chk was found to suppress VLA5 integrin-mediated cell spreading, but not cell attachment, throughout fibronectin (FN) stimulation. Deletion and point mutagenesis analyses of Chk showed that this suppression was dependent upon both the SH3 domain, which is responsible for membrane anchoring, and kinase activity. FN-induced cell spreading accompanied a sustained increase in Lyn activity with coincidental kinetics and the activation of Lyn was also suppressed by overexpression of Chk but not a Chk mutant lacking the SH3 domain. Expression of a truncated Lyn mutant lacking the kinase domain inhibited both cell spreading and Lyn activation upon stimulation with FN. These results suggest that sustained activation of Lyn, which is regulated by membrane-anchored Chk, plays a crucial role in VLA5-mediated cell spreading but not cell attachment to a FN substrate.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				I. Sato, Y. Obata, K. Kasahara, Y. Nakayama, Y. Fukumoto, T. Yamasaki, K. K. Yokoyama, T. Saito, and N. Yamaguchi Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain J. Cell Sci., April 1, 2009; 122(7): 965 - 975. [Abstract] [Full Text] [PDF]

				K. Kasahara, Y. Nakayama, Y. Nakazato, K. Ikeda, T. Kuga, and N. Yamaguchi Src Signaling Regulates Completion of Abscission in Cytokinesis through ERK/MAPK Activation at the Midbody J. Biol. Chem., February 23, 2007; 282(8): 5327 - 5339. [Abstract] [Full Text] [PDF]

				K. Kasahara, Y. Nakayama, K. Ikeda, Y. Fukushima, D. Matsuda, S. Horimoto, and N. Yamaguchi Trafficking of Lyn through the Golgi caveolin involves the charged residues on {alpha}E and {alpha}I helices in the kinase domain J. Cell Biol., June 7, 2004; 165(5): 641 - 652. [Abstract] [Full Text] [PDF]

				Y.-P. Chong, T. D. Mulhern, H.-J. Zhu, D. J. Fujita, J. D. Bjorge, J.-P. Tantiongco, N. Sotirellis, D. S. S. Lio, G. Scholz, and H.-C. Cheng A Novel Non-catalytic Mechanism Employed by the C-terminal Src-homologous Kinase to Inhibit Src-family Kinase Activity J. Biol. Chem., May 14, 2004; 279(20): 20752 - 20766. [Abstract] [Full Text] [PDF]

				S. Pereira and C. Lowell The Lyn Tyrosine Kinase Negatively Regulates Neutrophil Integrin Signaling J. Immunol., August 1, 2003; 171(3): 1319 - 1327. [Abstract] [Full Text] [PDF]

				N Yamaguchi, Y Nakayama, T Urakami, S Suzuki, T Nakamura, T Suda, and N Oku Overexpression of the Csk homologous kinase (Chk tyrosine kinase) induces multinucleation: a possible role for chromosome-associated Chk in chromosome dynamics J. Cell Sci., January 5, 2001; 114(9): 1631 - 1641. [Abstract] [PDF]

				J.-i. Tada, M. Omine, T. Suda, and N. Yamaguchi A Common Signaling Pathway Via Syk and Lyn Tyrosine Kinases Generated From Capping of the Sialomucins CD34 and CD43 in Immature Hematopoietic Cells Blood, June 1, 1999; 93(11): 3723 - 3735. [Abstract] [Full Text] [PDF]

				A. Mera, M. Suga, M. Ando, T. Suda, and N. Yamaguchi Induction of Cell Shape Changes through Activation of the Interleukin-3 Common beta  Chain Receptor by the RON Receptor-type Tyrosine Kinase J. Biol. Chem., May 28, 1999; 274(22): 15766 - 15774. [Abstract] [Full Text] [PDF]

				C. Bougeret, S. Jiang, I. Keydar, and H. Avraham Functional Analysis of Csk and CHK Kinases in Breast Cancer Cells J. Biol. Chem., August 31, 2001; 276(36): 33711 - 33720. [Abstract] [Full Text] [PDF]