期刊
IUBMB LIFE
卷 55, 期 12, 页码 653-660出版社
WILEY
DOI: 10.1080/152165401310001642216
关键词
protein kinase C; green fluorescent protein; fluorescent resonance energy transfer; translocation
资金
- NIDDK NIH HHS [P01 DK54441] Funding Source: Medline
- NIGMS NIH HHS [GM43154] Funding Source: Medline
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [P01DK054441] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM043154, R01GM043154] Funding Source: NIH RePORTER
Protein kinase C has been at the center of cell signaling since the discovery 25 years ago that it transduces signals that promote phospholipid hydrolysis. In recent years, the use of genetically encoded fluorescent reporters has enabled studies of the regulation of protein kinase C signaling in living cells. Advances in imaging techniques have unveiled unprecedented detail of the signal processing mechanics of protein kinase C, from the second messengers calcium and diacylglycerol that regulate protein kinase C activity, to the locations and kinetics of different protein kinase C isozymes, to the spatial and temporal dynamics of substrate phosphorylation by this key enzyme. This review discusses how fluorescence imaging studies have illuminated the fidelity with which protein kinase C transduces rapidly changing extracellular information into intracellular phosphorylation signals.
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