CPS1 accumulates at an aberrant late endosomal compartment in mutants of the COPIB subcomplex. CPS1 is not delivered to the vacuolar lumen in COPIb mutants. Only mutations in COPIb subunits have an effect upon CPS1 sorting, whereas in COPIf mutants CPS1 localizes to the vacuolar lumen
GFP-Cps1p accumulates in a prevacuolar compartment as well as on the limiting membrane of the vacuole in rps5WW1-3 cells with WW domain mutations. In rsp5L733S cells, GFP-Cps1p is detectable in the lumen of the vacuole, some is also found on the limiting membrane of the vacuole. In bsd2delta cells, GFP-Cps1p accumulates in the limiting membrane of the vacuole. In tul1delta cells sorting is also impaired. No defect in GFP-Cps1p vacuolar sorting in sna3delta cells
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GFP-Cps1p expressed in rsp5delta cells expressing wild-type or mutant HA-Rsp5p with WW domain mutations W257A, W359A, and W415A. GFP-Cps1p expressed in rsp5delta cells expressing HARsp5pWT, HA-rsp5pL733S or HA-rsp5G555D. GFP-Cps1p expressed in tul1delta cells, bsd2delta cells and sna3delta cells
sorting of Cps1p into the luminal vesicles of multivesicular bodies requires ubiquitination of their cytosolic domains by the ubiquitin ligases Rsp5p and/or Tul1p, whereas Sna3p, another integral membrane protein, does not require ubiquitination for entry into multivesicular bodies. Sna3p follows an ubiquitination-independent, but Rsp5p-mediated, sorting pathway to the vacuole