Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 12, Issue 12, Pages 3498-3508Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.R113.029819
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Funding
- National Institutes of Health [GM43154, P01 DK054441]
- UCSD Graduate Training Program in Cellular and Molecular Pharmacology through National Institute of General Medical Sciences [T32 GM007752]
- National Science Foundation Graduate Research Fellowship [DGE1144086]
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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.
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