Journal article
Ubiquitin-dependent sorting of integral membrane proteins for degradation in lysosomes
Current opinion in cell biology, Vol.19(4), pp.459-465
08/2007
DOI: 10.1016/j.ceb.2007.07.002
PMCID: PMC2046217
PMID: 17689064
Abstract
The pathways that deliver newly synthesized proteins that reside in lysosomes are well understood on comparison with our knowledge of how integral membrane proteins are sorted and delivered to the lysosome for degradation. Many membrane proteins are sorted to lysosomes following ubiquitination, which provides a sorting signal that can operate for sorting at the TGN (trans-Golgi network), at the plasma membrane or at the endosome for delivery into lumenal vesicles. Candidate multicomponent machines that can potentially move ubiquitinated integral membrane cargo proteins have been identified, but much work is still required to ascertain which of these candidates directly recognize ubiquitinated cargo and what they do with cargo after recognition. In the case of the machinery required for sorting into the lumenal vesicles of endosomes, other functions have also been determined including a link between sorting and movement of endosomes along microtubules.
Details
- Title: Subtitle
- Ubiquitin-dependent sorting of integral membrane proteins for degradation in lysosomes
- Creators
- Robert C Piper - University of IowaJ Paul Luzio - University of Cambridge
- Resource Type
- Journal article
- Publication Details
- Current opinion in cell biology, Vol.19(4), pp.459-465
- DOI
- 10.1016/j.ceb.2007.07.002
- PMID
- 17689064
- PMCID
- PMC2046217
- NLM abbreviation
- Curr Opin Cell Biol
- ISSN
- 0955-0674
- eISSN
- 1879-0410
- Grant note
- G9310915 / Medical Research Council 079895 / Wellcome Trust R01 GM58202 / NIGMS NIH HHS R01 GM058202-09 / NIGMS NIH HHS R01 GM058202 / NIGMS NIH HHS
- Language
- English
- Date published
- 08/2007
- Academic Unit
- Molecular Physiology and Biophysics; Medicine Administration; Internal Medicine
- Record Identifier
- 9984297493102771
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