C1 domains exposed: from diacylglycerol binding to protein-protein interactions.

  title={C1 domains exposed: from diacylglycerol binding to protein-protein interactions.},
  author={Francheska Col{\'o}n-Gonz{\'a}lez and Marcelo G Kazanietz},
  journal={Biochimica et biophysica acta},
  volume={1761 8},
C1 domains, cysteine-rich modules originally identified in protein kinase C (PKC) isozymes, are present in multiple signaling families, including PKDs, chimaerins, RasGRPs, diacylglycerol kinases (DGKs) and others. Typical C1 domains bind the lipid second messenger diacylglycerol (DAG) and DAG-mimetics such as phorbol esters, and are critical for governing association to membranes. On the contrary, atypical C1 domains possess structural determinants that impede phorbol ester/DAG binding. C1… CONTINUE READING
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