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The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
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.
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Sortilin belongs to a family of multiligand type-1 receptors with homology to the yeast receptor Vps10p.
“Sortilin belongs to a growing family of multiligand type-1 receptors with homology to the yeast receptor Vps10p.”
From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Marcusson et al., 1994
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Metadata
- Authors
- Marcusson, E. G., Horazdovsky, B. F., Cereghino, J. L., Gharakhanian, E., & Emr, S. D.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1994-05
- Volume
- 77
- Issue
- 4
- Pages
- 579-586
- ISSN
- 0092-8674
- Cited by
- 439
- References
- 0
- Language
- en
- Funders
- National Institutes of Health (GM32703, GM15638)
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