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Ubiquitin-dependent sorting of integral membrane proteins for degradation in lysosomes

Piper, Robert C, Luzio, J Paul·2007·Current Opinion in Cell Biology
DOI 10.1016/j.ceb.2007.07.002
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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.

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Research works printed but not linked: 64

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Metadata

Authors
Piper, R. C., & Luzio, J. P.
Venue
Current Opinion in Cell Biology
Publisher
Elsevier BV
Published
2007-08
Volume
19
Issue
4
Pages
459-465
ISSN
0955-0674
DOI
10.1016/j.ceb.2007.07.002
Cited by
151
References
2
Language
en
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