Abstract
The plasma membrane serves as a dynamic interface that relays information received at the cell surface into the cell. Lipid second messengers coordinate signaling on this platform by recruiting and activating kinases and phosphatases. Specifically, diacylglycerol and phosphatidylinositol 3,4,5-trisphosphate activate protein kinase C and Akt, respectively, which then phosphorylate target proteins to transduce downstream signaling. This review addresses how the spatiotemporal dynamics of protein kinase C and Akt signaling can be monitored using genetically encoded reporters and provides information on how the coordination of signaling at protein scaffolds or membrane microdomains affords fidelity and specificity in phosphorylation events.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Review
MeSH terms
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Animals
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Diglycerides / metabolism*
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Eukaryotic Cells / cytology
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Eukaryotic Cells / metabolism
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Gene Expression Regulation
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Humans
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Membrane Microdomains / chemistry
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Membrane Microdomains / metabolism*
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Phosphatidylinositol Phosphates / metabolism*
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Phosphoric Monoester Hydrolases / genetics
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Phosphoric Monoester Hydrolases / metabolism
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Phosphorylation
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Protein Kinase C / genetics
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Protein Kinase C / metabolism*
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Protein Processing, Post-Translational*
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Proto-Oncogene Proteins c-akt / genetics
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Proto-Oncogene Proteins c-akt / metabolism*
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Second Messenger Systems*
Substances
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1,2-diacylglycerol
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Diglycerides
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Phosphatidylinositol Phosphates
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phosphatidylinositol 3,4,5-triphosphate
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Proto-Oncogene Proteins c-akt
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Protein Kinase C
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Phosphoric Monoester Hydrolases