ESCRT-III recognition by VPS4 ATPases

Melissa D. Stuchell-Brereton, Jack J. Skalicky, Collin Kieffer, Mary Anne Karren, Sanaz Ghaffarian and Wesley I. Sundquist ()
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Melissa D. Stuchell-Brereton: Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA
Jack J. Skalicky: Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA
Collin Kieffer: Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA
Mary Anne Karren: Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA
Sanaz Ghaffarian: Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA
Wesley I. Sundquist: Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA

Nature, 2007, vol. 449, issue 7163, 740-744

Abstract: The microtubule interacting and tarnsport (MIT) domain of Vps4 binds conserved residues in the CHMP1-3 class of ESCRT-III proteins. These results reveal how Vps4 recognises substrates to facilitate membrane fission events required for viral release and endosomal vesicles

Date: 2007
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DOI: 10.1038/nature06172

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