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Article

Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae.

The Journal of cell biology - 1 May 1991

Redding K, Holcomb C, Fuller R S

Abstract excerpt

The Kex2 protein of the yeast Saccharomyces cerevisiae is a membrane-bound, Ca2(+)-dependent serine protease that cleaves the precursors of the mating pheromone alpha-factor and the M1 killer toxin at pairs of basic residues during their transport through the secretory pathway. To begin to characterize the intracellular locus of Kex2-dependent proteolytic processing, we have examined the subcellular distribution...

Topics

Cell Cycle
Cytoplasmic Granules
Endoplasmic Reticulum
Fluorescent Antibody Technique
Golgi Apparatus
Mitosis
Mutation
Proprotein Convertases
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Serine Endopeptidases

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Identifiers

PMID: 2016334
DOI: 10.1083/jcb.113.3.527
PMCID: PMC2288974

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2016334-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae.PMID 2016334Read ↗

Immunoisolation of Kex2p-containing organelles from yeast demonstrates colocalisation of three processing proteinases to a single Golgi compartment.Semantic proximity Read ↗

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The effects of clathrin inactivation on localization of Kex2 protease are independent of the TGN localization signal in the cytosolic tail of Kex2p.Semantic proximity Read ↗

The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating.Semantic proximity Read ↗

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