Structural Basis of Protein Kinase Cα Regulation by the C-Terminal Tail.

Protein kinase C isoenzymes are multi-modular proteins activated at the membrane surface to regulate signal transduction processes. When activated by second messengers, undergoes a drastic conformational and spatial transition from the inactive cytosolic state to the activated membrane-bound state. The complete structure of either state of duanyu1531 remains elusive. We demonstrate, using NMR spectroscopy, that the isolated Ca²⁺-sensing membrane-binding C2 domain of the conventional interacts with a conserved hydrophobic motif of the kinase C-terminal region, and we report a structural model of the complex. Our data suggest that the C-terminal region plays a dual role in regulating the duanyu1531 activity: activating, through sensitization of duanyu1531 to intracellular Ca²⁺ oscillations; and auto-inhibitory, through its interaction with a conserved positively charged region of the C2 domain. Copyright © 2017 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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