Phosphoproteomic analysis of protein kinase C signaling in Saccharomyces cerevisiae reveals Slt2 mitogen-activated protein kinase (MAPK)-dependent phosphorylation of eisosome core components.

doi:10.1074/mcp.M112.020438

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Article

Phosphoproteomic analysis of protein kinase C signaling in Saccharomyces cerevisiae reveals Slt2 mitogen-activated protein kinase (MAPK)-dependent phosphorylation of eisosome core components.

Molecular & cellular proteomics : MCP - 1 Mar 2013

Mascaraque Victoria, Hernáez María Luisa, Jiménez-Sánchez María, Hansen Rasmus, Gil Concha, Martín Humberto, Cid Víctor J, Molina María

Abstract excerpt

The cell wall integrity (CWI) pathway of the model organism Saccharomyces cerevisiae has been thoroughly studied as a paradigm of the mitogen-activated protein kinase (MAPK) pathway. It consists of a classic MAPK module comprising the Bck1 MAPK kinase kinase, two redundant MAPK kinases (Mkk1 and Mkk2), and the Slt2 MAPK. This module is activated under a variety of stimuli related to cell wall homeostasis by Pkc1,...

Topics

Amino Acid Sequence
Binding Sites
Blotting, Western
Cell Membrane
Cell Wall
Mass Spectrometry
Microscopy, Fluorescence
Mitogen-Activated Protein Kinases
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phosphopeptides

Phosphoproteins

Phosphorylation

Protein Kinase C

Proteome

Proteomics

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Source

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Identifiers

PMID: 23221999
DOI: 10.1074/mcp.M112.020438
PMCID: PMC3591651

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-23221999-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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