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Originally published In Press as doi:10.1074/jbc.C000106200 on March 20, 2000
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J Biol Chem, Vol. 275, Issue 19, 14005-14008, May 12, 2000

ACCELERATED PUBLICATION
Suppressor of Cytokine Signaling-1 Inhibits VAV Function through Protein Degradation*

Paulo De SepulvedaDagger §, Subburaj IlangumaranDagger §||, and Robert RottapelDagger **Dagger Dagger

From the Dagger  Ontario Cancer Institute, Princess Margaret Hospital, 610 University Avenue, Toronto ON M5G 2M9, Canada and ** Department of Immunology and Medical Biophysics and Department of Medicine, University of Toronto, Toronto, M5G 2M9 Canada

Suppressor of cytokine signaling-1 (SOCS1) is an inducible Src homology 2 (SH2)-containing protein that negatively regulates cytokine and growth factor signaling required during thymic development. Recent evidence indicates that SOCS1 interacts with elongins B and C, which are components of a ubiquitin ligase complex, VCB (VHL/elonginC/B), based on the VHL (von Hippel Lindau) tumor suppressor protein. SOCS1 has previously been shown to operate as an inhibitor of Janus kinases. Here we show that SOCS1 has the distinct function of targeting the hematopoietic specific guanine nucleotide exchange factor, VAV, for ubiquitin-mediated protein degradation. VAV and SOCS1 form a protein complex through interactions between the VAV NH2-terminal regulatory region and the SH2 domain of SOCS1 in a phosphotyrosine-independent manner. SOCS1 decreases the steady state levels of cotransfected VAV and onco-VAV and reduces the focus forming activity of onco-VAV. SOCS1 stimulates the polyubiquitination of VAV proteins in vivo, which was stabilized by proteasomal inhibitors. These results suggest that SOCS1 programs VAV degradation by acting as a substrate-specific recognition component of a VCB-like ubiquitin ligase complex.

* This work was supported by grants from the Medical Research Council of Canada (MRC) and the National Cancer Institute of Canada. 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.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.

§ These authors have contributed equally to this work.

Supported by fellowships from the Leukemia Research Fund of Canada and the MRC. Present address: INSERM U119, Institut Paoli-Calmettes, 27 Blvd. Leï Roure, 13009 Marseille, France.

|| Supported by an MRC postdoctoral fellowship.

Dagger Dagger Senior Research Scholar of the Arthritis Society of Canada. To whom correspondence should be addressed. Tel.: 416-946-2233; Fax: 416-946-2984; E-mail: Rottapel@oci.utoronto.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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