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Targeting of protein kinase Calpha to caveolae.

作者信息

Mineo C, Ying Y S, Chapline C, Jaken S, Anderson R G

机构信息

Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9039, USA.

出版信息

J Cell Biol. 1998 May 4;141(3):601-10. doi: 10.1083/jcb.141.3.601.

DOI:10.1083/jcb.141.3.601
PMID:9566962
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2132740/
Abstract

Previously, we showed caveolae contain a population of protein kinase Calpha (PKCalpha) 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 PKCalpha and measured the interaction of recombinant PKCalpha with these membranes. PKCalpha 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 PKCalpha-binding protein identified as sdr (serum deprivation response) was isolated by interaction cloning and localized to caveolae. Antibodies against sdr inhibited PKCalpha binding. A 100-amino acid sequence from the middle of sdr competitively blocked PKCalpha 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.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/3e391fba666f/JCB29449.f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/18f99a854310/JCB29449.f1ac.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/75c5bceb90b3/JCB29449.f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/31c9810fa311/JCB29449.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/855da89f5230/JCB29449.f4c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/46c5ee5756ca/JCB29449.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/89c5094b9abf/JCB29449.f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/a9f53ffca790/JCB29449.f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/2cab136dbf2a/JCB29449.f8ad.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/3e391fba666f/JCB29449.f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/18f99a854310/JCB29449.f1ac.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/75c5bceb90b3/JCB29449.f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/31c9810fa311/JCB29449.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/855da89f5230/JCB29449.f4c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/46c5ee5756ca/JCB29449.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/89c5094b9abf/JCB29449.f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/a9f53ffca790/JCB29449.f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/2cab136dbf2a/JCB29449.f8ad.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/efe6/2132740/3e391fba666f/JCB29449.f9.jpg

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Trends Cell Biol. 1994 Jul;4(7):231-5. doi: 10.1016/0962-8924(94)90114-7.
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The caveolae membrane system.小窝膜系统。
Annu Rev Biochem. 1998;67:199-225. doi: 10.1146/annurev.biochem.67.1.199.
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Caveolin interaction with protein kinase C. Isoenzyme-dependent regulation of kinase activity by the caveolin scaffolding domain peptide.小窝蛋白与蛋白激酶C的相互作用。小窝蛋白支架结构域肽对激酶活性的同工酶依赖性调节。
Ann Med. 2025 Dec;57(1):2457526. doi: 10.1080/07853890.2025.2457526. Epub 2025 Jan 31.
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Spatiotemporal control of kinases and the biomolecular tools to trace activity.激酶的时空控制以及用于追踪活性的生物分子工具。
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G protein-coupled estrogen receptor (GPER) in the dorsal hippocampus regulates memory consolidation in gonadectomized male mice, likely via different signaling mechanisms than in female mice.背侧海马中的 G 蛋白偶联雌激素受体 (GPER) 在去势雄性小鼠中调节记忆巩固,其可能通过与雌性小鼠不同的信号机制来实现。
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Unraveling the Cave: A Seventy-Year Journey into the Caveolar Network, Cellular Signaling, and Human Disease.揭开洞穴的奥秘:七十载探索陷窝网络、细胞信号转导与人类疾病
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