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Updated: Apr 30, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
Published on: October 4, 2024
Ready, set, go! How protein kinase C manages dynamic signaling
1Department of Biochemistry & Molecular Biology, Indiana University School of Medicine-South Bend, South Bend, IN 46617, USA; Department of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Abstract:
In this issue of Chemistry & Biology, Antal and colleagues describe how phosphorylation optimizes the signaling range of protein kinase C (PKC) isoforms. Priming of these enzymes regulates intramolecular conformational changes, which reduces access to their diacylglycerol (DAG) binding C1 domains.
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