Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein.

doi:10.1074/jbc.M802140200

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Article

Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein.

The Journal of biological chemistry - 5 Sept 2008

Greaves Jennifer, Salaun Christine, Fukata Yuko, Fukata Masaki, Chamberlain Luke H

Abstract excerpt

Cysteine-string protein (CSP) is an extensively palmitoylated DnaJ-family chaperone, which exerts an important neuroprotective function. Palmitoylation is required for the intracellular sorting and function of CSP, and thus it is important to understand how this essential modification of CSP is regulated. Recent work identified 23 putative palmitoyl transferases containing a conserved DHHC domain in mammalian...

Topics

Acyltransferases
Animals
Brefeldin A
Cell Membrane
Endoplasmic Reticulum
Golgi Apparatus
HSP40 Heat-Shock Proteins
Humans
Lipoylation
Membrane Proteins
Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Neuroprotective Agents

PC12 Cells

Protein Structure, Tertiary

Protein Synthesis Inhibitors

Protein Transport

Rats

Source

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Identifiers

PMID: 18596047
DOI: 10.1074/jbc.M802140200
PMCID: PMC2882233

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