Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p.

doi:10.1083/jcb.151.2.297

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Article

Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p.

The Journal of cell biology - 16 Oct 2000

Nothwehr S F, Ha S A, Bruinsma P

Abstract excerpt

Resident late-Golgi membrane proteins in Saccharomyces cerevisiae are selectively retrieved from a prevacuolar-endosomal compartment, a process dependent on aromatic amino acid-based sorting determinants on their cytosolic domains. The formation of retrograde vesicles from the prevacuolar compart...

Topics

Alkaline Phosphatase
Carrier Proteins
Cell Polarity
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
Endosomes
Fungal Proteins
Golgi Apparatus
Membrane Proteins
Models, Biological
Mutation
Protein Sorting Signals

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Structure, Tertiary

Protein Transport

Receptors, Cell Surface

Recombinant Fusion Proteins

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Signal Recognition Particle

Source

Open in PubMed Open full text

Identifiers

PMID: 11038177
DOI: 10.1083/jcb.151.2.297
PMCID: PMC2192648

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-11038177-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p.PMID 11038177Read ↗

Distinct domains within Vps35p mediate the retrieval of two different cargo proteins from the yeast prevacuolar/endosomal compartment.Semantic proximity Read ↗

Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment.Semantic proximity Read ↗

env1 Mutant of VPS35 gene exhibits unique protein localization and processing phenotype at Golgi and lysosomal vacuole in Saccharomyces cerevisiae.Semantic proximity Read ↗

Structural features of vps35p involved in interaction with other subunits of the retromer complex.Semantic proximity Read ↗

Vps26p, a component of retromer, directs the interactions of Vps35p in endosome-to-Golgi retrieval.Semantic proximity Read ↗

Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase.Semantic proximity Read ↗

Dominant-negative behavior of mammalian Vps35 in yeast requires a conserved PRLYL motif involved in retromer assembly.Semantic proximity Read ↗

Arabidopsis VPS35, a retromer component, is required for vacuolar protein sorting and involved in plant growth and leaf senescence.Semantic proximity Read ↗

Vps10p transport from the trans-Golgi network to the endosome is mediated by clathrin-coated vesicles.Semantic proximity Read ↗

The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene.Semantic proximity Read ↗

Identification of a conserved motif required for Vps35p/Vps26p interaction and assembly of the retromer complex.Semantic proximity Read ↗

A novel immunodetection screen for vacuolar defects identifies a unique allele of VPS35 in S. cerevisiae.Semantic proximity Read ↗

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