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Originally published In Press as doi:10.1074/jbc.M100606200 on March 8, 2001

J. Biol. Chem., Vol. 276, Issue 22, 19332-19339, June 1, 2001
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Sorting Nexin 6, a Novel SNX, Interacts with the Transforming Growth Factor-beta Family of Receptor Serine-Threonine Kinases*

W. Tony Parks, David B. Frank, Carla Huff, Carol Renfrew HaftDagger , Jennifer Martin§, Xianwang Meng§, Mark P. de Caestecker, James G. McNally, Amit Reddi, Simeon I. TaylorDagger , Anita B. Roberts, Tongwen Wang§||, and Robert J. Lechleider**

From the Laboratory of Cell Regulation and Carcinogenesis, NCI, the Dagger  Diabetes Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, and the § Department of Surgery, Massachusetts General Hospital, Department of Genetics, Harvard Medical School, Boston, Massachusetts 02114

Sorting nexins (SNX) comprise a family of proteins with homology to several yeast proteins, including Vps5p and Mvp1p, that are required for the sorting of proteins to the yeast vacuole. Human SNX1, -2, and -4 have been proposed to play a role in receptor trafficking and have been shown to bind to several receptor tyrosine kinases, including receptors for epidermal growth factor, platelet-derived growth factor, and insulin as well as the long form of the leptin receptor, a glycoprotein 130-associated receptor. We now describe a novel member of this family, SNX6, which interacts with members of the transforming growth factor-beta family of receptor serine-threonine kinases. These receptors belong to two classes: type II receptors that bind ligand, and type I receptors that are subsequently recruited to transduce the signal. Of the type II receptors, SNX6 was found to interact strongly with ActRIIB and more moderately with wild type and kinase-defective mutants of Tbeta RII. Of the type I receptors, SNX6 was found to interact only with inactivated Tbeta RI. SNXs 1-4 also interacted with the transforming growth factor-beta receptor family, showing different receptor preferences. Conversely, SNX6 behaved similarly to the other SNX proteins in its interactions with receptor tyrosine kinases. Strong heteromeric interactions were also seen among SNX1, -2, -4, and -6, suggesting the formation in vivo of oligomeric complexes. These findings are the first evidence for the association of the SNX family of molecules with receptor serine-threonine kinases.

* 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.

To whom correspondence should be addressed. Tel.: 301-496-5391; Fax: 301-496-8395; E-mail: robertsa@dce41.nci.nih.gov.

|| Present address: Virginia Mason Research Center, 1201 9th Ave., Seattle, WA 98101, and the Dept. of Immunology, University of Washington, Seattle, WA 98195.

** Present address: Dept. of Pharmacology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Rd., Bethesda, MD 20814.

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