Journal article
A single ubiquitin is sufficient for cargo protein entry into MVBs in the absence of ESCRT ubiquitination
The Journal of cell biology, Vol.192(2), pp.229-242
01/24/2011
DOI: 10.1083/jcb.201008121
PMCID: PMC3172180
PMID: 21242292
Abstract
ESCRTs (endosomal sorting complexes required for transport) bind and sequester ubiquitinated membrane proteins and usher them into nnultivesicular 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. Moreover, by fusing the catalytic domain of deubiquitinating peptidases onto ESCRTs, we could block ESCRT ubiquitination and the sorting of proteins that undergo Rsp5-dependent ubiquitination. Yet, proteins fused to a single Ub moiety were efficiently delivered to the MVB lumen, which strongly indicates that a single Ub is sufficient in sorting MVBs in the absence of ESCRT ubiquitination.
Details
- Title: Subtitle
- A single ubiquitin is sufficient for cargo protein entry into MVBs in the absence of ESCRT ubiquitination
- Creators
- Daniel K. Stringer - University of IowaRobert C. Piper - University of Iowa
- Resource Type
- Journal article
- Publication Details
- The Journal of cell biology, Vol.192(2), pp.229-242
- DOI
- 10.1083/jcb.201008121
- PMID
- 21242292
- PMCID
- PMC3172180
- NLM abbreviation
- J Cell Biol
- ISSN
- 0021-9525
- eISSN
- 1540-8140
- Publisher
- Rockefeller Univ Press
- Number of pages
- 14
- Grant note
- R01GM058202 / NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS) R01GM58202 / National Institutes of Health; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA American Hearth Association; American Heart Association
- Language
- English
- Date published
- 01/24/2011
- Academic Unit
- Molecular Physiology and Biophysics; Medicine Administration; Internal Medicine
- Record Identifier
- 9984297504002771
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