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Prepublished online as a Blood First Edition Paper on June 28, 2002; DOI 10.1182/blood-2001-11-0032. This Article Full Text (PDF) All Versions of this Article: 2001-11-0032v1 100/12/3968    most recent Alert me when this article is cited Alert me if a correction is posted 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 Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Nishihara, H. Articles by Nagashima, K. Search for Related Content PubMed PubMed Citation Articles by Nishihara, H. Articles by Nagashima, K. Social Bookmarking                   What's this? Submitted November 26, 2001 Accepted May 10, 2002 DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines Hiroshi Nishihara, Masae Maeda, Atsushi Oda, Masumi Tsuda, Hirofumi Sawa, Shinya Tanaka*, and Kazuo Nagashima Laboratory of Molecular and Cellular Pathology, Hokkaido University School of Medicine, Sapporo, Japan; CREST, Japan Science and Technology Cooperation, Japan Laboratory of Environmental Biology, Hokkaido University School of Medicine, Sapporo, Japan * Corresponding author; email: sitanaka{at}patho2.med.hokudai.ac.jp. The CDM family of proteins has been shown to play a pivotal role in the integrin-mediated signalling pathway under the regulation of an adaptor molecule c-Crk-II in adherent cells. Recently, hematopoietic cell-specific CDM protein DOCK2 has been shown to be indispensable for lymphocyte migration (Fukui, Y., et al., Nature, 412, 826-831, 2001). However, the regulatory mechanism for DOCK2 is still unknown because DOCK2 lacks a c-Crk-II binding consensus motif. In this study, we demonstrated that DOCK2 bound to CrkL which is exclusively present in hematopoietic cells both in vivo and in vitro, as well as two separate regions of DOCK2 were found to contribute to its binding to SH3 domain of CrkL. Colocalization of DOCK2 with CrkL and F-actin was shown by immunocytochemical analysis using Jurkat cells. We also found that CrkL-induced activation of small GTPase Rac1 was significantly inhibited by the DOCK2-dCS mutant in 293T cells. Furthermore, the association of DOCK2 and Vav, the guanine-nucleotide exchanging factor (GEF) for Rac1, was demonstrated in Jurkat cells. Finally, the stable expression of DOCK2-dCS mutant in Jurkat cells was shown to reduce cell attachment. These data suggest the presence of a novel protein complex of CrkL, DOCK2, and Vav to regulate Rac1 in heukemia cell lines. 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