Sorting in the endosomal system in yeast and animal cells

Current Opinion in Cell Biology

Volumn 12, Issue 4, 2000, Pages 457-466

  Lemmon, Sandra K ^a   Traub, Linton M ^b  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; UBIQUITIN;

ANIMAL CELL; ENDOSOME; INVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN TARGETING; REVIEW; YEAST;

ANIMALIA; FUNGI;

EID: 0033939453     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00117-4     Document Type: Review

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93. •]. While internalization is normal, mutant Rcy1p leads to accumulation of endocytic markers in an early endosomal compartment, preventing both recycling to the cell surface and transport on to the prevacuole. Interestingly, several members of the F-box family of proteins mediate ubiquitination of substrates as components of SKP1/cullin/F-box ubiquitin ligase complexes. Therefore, Rcy1p may function in a ubiquitination pathway that regulates transport in the endosomal system.