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Papers In Press, published online ahead of print March 22, 2006
J. Biol. Chem, 10.1074/jbc.M600433200
Submitted on January 17, 2006
Revised on March 10, 2006
Accepted on March 22, 2006
Medical Pharmacology & Physiology, University of Missouri School of Medicine, Columbia, MO 65212
Corresponding Author: davismj{at}health.missouri.edu
L-type, voltage-gated Ca2+ channels (CaL) play critical roles in brain and muscle cell excitability. Here we show that currents through heterologously expressed neuronal and smooth muscle CaL channel isoforms are acutely potentiated following 
5
1 integrin activation. Only the a(sub1C} pore-forming channel subunit is critical for this process. Truncation and site-directed mutagenesis strategies reveal that regulation of Cav1.2 by 51 integrin requires phosphorylation of a1C C-terminal residues S1901 and Y2122. These sites are known to be phosphorylated by PKA and c-Src, respectively, and are conserved between rat neuronal (Cav1.2c) and smooth muscle (Cav1.2b) isoforms. Kinase assays are consistent with phosphorylation of these two residues by PKA and c-Src. Following 51 integrin activation, native CaL channels in rat arteriolar smooth muscle exhibit potentiation that is completely blocked by combined PKA and Src inhibition. Our results demonstrate that integrin-ECM interactions are a common mechanism for the acute regulation of CaL channels in brain and muscle. These findings are consistent with the growing recognition of the importance of integrin-channel interactions in cellular responses to injury and the acute control of synaptic and blood vessel function.
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