Journal
CURRENT OPINION IN CELL BIOLOGY
Volume 19, Issue 4, Pages 459-465Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.ceb.2007.07.002
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Funding
- MRC [G9310915] Funding Source: UKRI
- Medical Research Council [G9310915] Funding Source: researchfish
- Medical Research Council [G9310915] Funding Source: Medline
- NIGMS NIH HHS [R01 GM58202, R01 GM058202, R01 GM058202-09] Funding Source: Medline
- Wellcome Trust [079895] Funding Source: Medline
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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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