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Originally published In Press as doi:10.1074/jbc.M006250200 on October 12, 2000

J. Biol. Chem., Vol. 276, Issue 4, 2451-2458, January 26, 2001
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SHIP1, an SH2 Domain Containing Polyinositol-5-phosphatase, Regulates Migration through Two Critical Tyrosine Residues and Forms a Novel Signaling Complex with DOK1 and CRKL*

Martin SattlerDagger , Shalini Verma, Yuri B. Pride, Ravi Salgia, Larry R. Rohrschneider§, and James D. Griffin

From the Dana-Farber Cancer Institute, Department of Adult Oncology, Harvard Medical School, Boston, Massachusetts 02115 and the § Fred Hutchinson Cancer Research Center, Department of Basic Science, Seattle, Washington 98109

SHIP1 is an SH2 domain containing inositol-5-phosphatase that appears to be a negative regulator of hematopoiesis. The tyrosine kinase oncogene BCR/ABL drastically reduces expression of SHIP1. The major effect of re-expressing SHIP1 in BCR/ABL-transformed cells is reduction of hypermotility. To investigate the potential signaling pathways involving SHIP1 in hematopoietic cells, we overexpressed SHIP1 in a murine BCR/ABL-transformed Ba/F3 cell line and identified SHIP1-associated proteins. SHIP1 was found to form a novel signaling complex with BCR/ABL that includes DOK1 (p62DOK), phosphatidylinositol 3-kinase (PI3K), and CRKL, each of which has been previously shown to regulate migration in diverse cell types. We found that DOK1 binds directly through its PTB domain to SHIP1. Direct interaction of SHIP1 with CRKL was mediated through the CRKL-SH2 domain. Co-precipitation experiments suggest that Tyr917 and Tyr1020 in SHIP1 are likely to mediate interactions with DOK1. In contrast to wild type SHIP1, expression of tyrosine mutant SHIP1 by transient transfection did not alter migration. PI3K was likely linked to this complex by CRKL. Thus, this complex may serve to generate a very specific set of phosphoinositol products, possibly involved in regulating migration. Overall, these data suggest that proteins that interact with SHIP1 through Tyr917 and Tyr1020, such as DOK1 and SHC, are likely to be involved in the regulation of SHIP1 dependent migration.

* This work was supported by the Leukemia Research Foundation (to M. S.), and National Institutes of Health Grants CA78348 (to R. S.), CA82499 (to L. R. R.), and DK50654 (to J. D. G.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 617-632-4382; Fax: 617-632-4388; E-mail: martin_sattler@dfci.harvard.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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