The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene

Eric G. Marcusson, Bruce F. Horazdovsky, Joan Lin Cereghino, Editte Gharakhanian, Scott D. Emr

Research output: Contribution to journalArticlepeer-review

380 Scopus citations

Abstract

The S. cerevisiae VPS10 (vacuolar protein sorting) gene encodes a type I transmembrane protein of 1577 amino acids required for the sorting of the soluble vacuolar protein carboxypeptidase Y (CPY). Mutations in VPS10 result in the selective missorting and secretion of CPY; all other vacuolar proteins tested are delivered to the vacuole in vps10 mutants. Chemical cross-linking studies demonstrate that Vps10p and the Golgi-modified precursor form of CPY directly interact. A single amino acid change in the CPY vacuolar sorting signal prevents this interaction. Vps10p also interacts with a hybrid protein containing the CPY sorting signal fused to the normally secreted enzyme invertase. Subcellular fractionation indicates that the majority of Vps10p is localized to a late Golgi compartment where vacuolar proteins are sorted. We propose that VPS10 encodes a CPY sorting receptor that executes multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment.

Original languageEnglish (US)
Pages (from-to)579-586
Number of pages8
JournalCell
Volume77
Issue number4
DOIs
StatePublished - May 20 1994

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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