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Papers In Press, published online ahead of print 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
J. Biol. Chem, 10.1074/jbc.M600433200
Submitted on January 17, 2006
Revised on March 10, 2006
Accepted on March 22, 2006
Integrin receptor activation triggers converging regulation of Cav1.2 calcium channels by c-Src and PKA pathways
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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