Sorting Nexin 6, a Novel SNX, Interacts with the Transforming Growth Factor-β Family of Receptor Serine-Threonine Kinases

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 s...

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Published in:The Journal of biological chemistry 2001-06, Vol.276 (22), p.19332
Main Authors: W. Tony Parks, David B. Frank, Carla Huff, Carol Renfrew Haft, Jennifer Martin, Xianwang Meng, Mark P. de Caestecker, James G. McNally, Amit Reddi, Simeon I. Taylor, Anita B. Roberts, Tongwen Wang, Robert J. Lechleider
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container_issue 22
container_start_page 19332
container_title The Journal of biological chemistry
container_volume 276
creator W. Tony Parks
David B. Frank
Carla Huff
Carol Renfrew Haft
Jennifer Martin
Xianwang Meng
Mark P. de Caestecker
James G. McNally
Amit Reddi
Simeon I. Taylor
Anita B. Roberts
Tongwen Wang
Robert J. Lechleider
description 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-β 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 TβRII. Of the type I receptors, SNX6 was found to interact only with inactivated TβRI. SNXs 1–4 also interacted with the transforming growth factor-β 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.
doi_str_mv 10.1074/jbc.M100606200
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title Sorting Nexin 6, a Novel SNX, Interacts with the Transforming Growth Factor-β Family of Receptor Serine-Threonine Kinases
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