A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies

Fulvio Reggiori, Hugh R B Pelham

OnderzoeksoutputAcademicpeer review

149 Citaten (Scopus)


Membrane proteins with transmembrane domains (TMDs) that contain polar residues exposed to the lipid bilayer are selectively sorted into multivesicular bodies (MVBs) and delivered to the yeast vacuole. Sorting of some, although not all, proteins into these structures is mediated by ubiquitination. We have identified a transmembrane ubiquitin ligase, Tul1, that is resident in the Golgi apparatus and is required for the ubiquitination of proteins with polar TMDs, including vacuolar proteins such as carboxypeptidase S. We suggest that Tul1 provides quality control, identifying misfolded membrane proteins and marking them for transport to endosomes and degradation in the vacuole.

Originele taal-2English
Pagina's (van-tot)117-23
Aantal pagina's7
TijdschriftNature Cell Biology
Nummer van het tijdschrift2
StatusPublished - feb.-2002
Extern gepubliceerdJa

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