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A single ubiquitin is sufficient for cargo protein entry into MVBs in the absence of ESCRT ubiquitination.

J Cell Biol.. 2011-01;  192(2):229 - 242
Daniel K. Stringer and Robert C. Piper. Molecular Physiology and Biophysics, University of Iowa, Iowa City, IA 52246, USA.
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摘要

ESCRTs (endosomal sorting complexes required for transport) bind and sequester ubiquitinated membrane proteins and usher them into multivesicular bodies (MVBs). As Ubiquitin (Ub)-binding proteins, ESCRTs themselves become ubiquitinated. However, it is unclear whether this regulates a critical aspect of their function or is a nonspecific consequence of their association with the Ub system. We investigated whether ubiquitination of the ESCRTs was required for their ability to sort cargo into the MVB lumen. Although we found that Rsp5 was the main Ub ligase responsible for ubiquitination of ESCRT-0, elimination of Rsp5 or elimination of the ubiquitinatable lysines within ESCRT-0 did not affect MVB sorting. Moreove... More

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