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Published online
doi:10.1083/jcb.200811130
The Journal of Cell Biology, Vol. 185, No. 2, 213-224
The Rockefeller University Press, 0021-9525 $30.00
© Shields et al.
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ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting



S. Brookhart Shields1, Andrea J. Oestreich2, Stanley Winistorfer1, Doris Nguyen2, Johanna A. Payne2, David J. Katzmann2, and Robert Piper1

1 Department of Molecular Physiology and Biophysics, University of Iowa, Iowa City, IA 52240
2 Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905

Correspondence to David J. Katzmann: katzmann.david{at}mayo.edu; or Robert Piper: Robert-piper{at}uiowa.edu

Ubiquitin (Ub) sorting receptors facilitate the targeting of ubiquitinated membrane proteins into multivesicular bodies (MVBs). Ub-binding domains (UBDs) have been described in several endosomal sorting complexes required for transport (ESCRT). Using available structural information, we have investigated the role of the multiple UBDs within ESCRTs during MVB cargo selection. We found a novel UBD within ESCRT-I and show that it contributes to MVB sorting in concert with the known UBDs within the ESCRT complexes. These experiments reveal an unexpected level of coordination among the ESCRT UBDs, suggesting that they collectively recognize a diverse set of cargo rather than act sequentially at discrete steps.

S.B. Shields and A.J. Oestreich contributed equally to this paper.

Abbreviations used in this paper: CPY, carboxypeptidase Y; ESCRT, endosomal sorting complexes required for transport; DIC, differential interference contrast; HSQC, heteronuclear single quantum coherence; MVB, multivesicular body; NMR, nuclear magnetic resonance; NZF, Npl4 zinc finger; TAP, tandem affinity purification; Ub, ubiquitin; UBD, Ub-binding domain; UEV, Ub E2 variant; UIM, Ub-interacting motif.

© 2009 Shields et al.
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