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Targeting of Protein Kinase Cα to Caveolae

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Mineo, Chieko, Ying, Yun-Shu, Chapline, Christine, Jaken, Susan, Anderson, Richard G.W.·1998·The Journal of Cell Biology

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.

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Metadata

Authors
Mineo, C., Ying, Y.-S., Chapline, C., Jaken, S., & Anderson, R. G. W.
Venue
The Journal of Cell Biology
Published
1998-05-04
Volume
141
Issue
3
Pages
601-610
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W1923109334
Cited by
186
References
0
FWCI
3.28
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Targeting of Protein Kinase Cα to Caveolae. https://app.cochat.ai/papers/10.1083/jcb.141.3.601
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Mineo, C., Ying, Y.-S., Chapline, C., Jaken, S., & Anderson, R. G. W. (1998). Targeting of Protein Kinase Cα to Caveolae. The Journal of Cell Biology. https://doi.org/10.1083/jcb.141.3.601

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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