Acidic di-leucine motif essential for AP-3-dependent sorting and restriction of the functional specificity of the Vam3p vacuolar t-SNARE.

doi:10.1083/jcb.142.4.913

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Article

Acidic di-leucine motif essential for AP-3-dependent sorting and restriction of the functional specificity of the Vam3p vacuolar t-SNARE.

The Journal of cell biology - 24 Aug 1998

Darsow T, Burd C G, Emr S D

Abstract excerpt

The transport of newly synthesized proteins through the vacuolar protein sorting pathway in the budding yeast Saccharomyces cerevisiae requires two distinct target SNAP receptor (t-SNARE) proteins, Pep12p and Vam3p. Pep12p is localized to the pre-vacuolar endosome and its activity is required for...

Topics

Adaptor Proteins, Vesicular Transport
Alkaline Phosphatase
Biological Transport
Carboxypeptidases
Cathepsin A
Endosomes
Fungal Proteins
Leucine
Membrane Proteins
Monomeric Clathrin Assembly Proteins
Mutation
Nerve Tissue Proteins
Phosphoproteins
Qa-SNARE Proteins
SNARE Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 9722605
DOI: 10.1083/jcb.142.4.913
PMCID: PMC2132875

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9722605-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Vesicle-Associated Membrane Protein 3