Targeting of protein kinase Cα to caveolae

Chieko Mineo, Yun Shu Ying, Christine Chapline, Susan Jaken, Richard G W Anderson

Research output: Contribution to journalArticlepeer-review

155 Scopus citations

Abstract

Previously, we showed caveolae contain a population of protein kinase Cα (PKCα) that appears to regulate membrane invagination. We now report that multiple PKC isoenzymes are enriched in caveolae of unstimulated fibroblasts. To understand the mechanism of PKC targeting, we prepared caveolae lacking PKCα and measured the interaction of recombinant PKCα with these membranes. PKCα bound with high affinity and specificity to caveolae membranes. Binding was calcium dependent, did not require the addition of factors that activate the enzyme, and involved the regulatory domain of the molecule. A 68-kD PKCα-binding protein identified as sdr (serum deprivation response) was isolated by interaction cloning and localized to caveolae. Antibodies against sdr inhibited PKCα binding. A 100-amino acid sequence from the middle of sdr competitively blocked PKCα binding while flanking sequences were inactive. Caveolae appear to be a membrane site where PKC enzymes are organized to carry out essential regulatory functions as well as to modulate signal transduction at the cell surface.

Original languageEnglish (US)
Pages (from-to)601-610
Number of pages10
JournalJournal of Cell Biology
Volume141
Issue number3
DOIs
StatePublished - May 4 1998

ASJC Scopus subject areas

  • Cell Biology

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