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Published online
doi:10.1083/jcb.200903013
The Journal of Cell Biology, Vol. 185, No. 2, 185-187
The Rockefeller University Press, 0021-9525 $30.00
© Hurley et al.
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The circuitry of cargo flux in the ESCRT pathway



James H. Hurley and Xuefeng Ren

Laboratory of Molecular Biology, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, MD 20892

Correspondence to James H. Hurley: hurley{at}helix.nih.gov

The endosomal sorting complex required for transport (ESCRT) complexes sort ubiquitinated membrane proteins into multivesicular bodies, which is a key step in the lysosomal degradation pathway. Shields et al. (Shields, S.B., A.J. Oestreich, S. Winistorfer, D. Nguyen, J.A. Payne, D.J. Katzmann, and R. Piper. 2009. J. Cell Biol. 185:213–224) identify a new ubiquitin-binding site in ESCRT-I and provide evidence that the upstream ESCRT-I and -II complexes sort cargo in parallel rather than in series.



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ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting
S. Brookhart Shields, Andrea J. Oestreich, Stanley Winistorfer, Doris Nguyen, Johanna A. Payne, David J. Katzmann, and Robert Piper
J. Cell Biol. 2009 185: 213-224. [Abstract] [Full Text] [PDF]



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