Alternative splicing of Cav1.3 in the mouse

L‐type voltage‐gated Ca2+ channel Cav1.3, which is encoded by CACNA1D , is one of four poreforming 1α‐subunits and it has been shown to undergo alternative splicing. Mutations of CACNA1D have been associated with neurological disorders such as Parkinson's Disease and Epilepsy. Previous studies have shown that a Calmodulin‐IQ domain present in some splicing isoforms of CACNA1D is critical for Cav1.3 binding affinity to the pharmaceutical inhibitor drug DHP. Our results further characterize the alternative splicing of Cav1.3 for the development of further potential clinical applications. We were able to confirm four alternatively spliced regions, E8–E11, E12–E15, E32–36, and E46–E48 in Cacna1d . By semi‐quantitative RT‐PCR analysis, we found alternatively spliced variants of Cacna1d that were expressed at higher levels in brain‐derived tissues when compared to non‐brain derived tissues. Given how previously characterized alternatively spliced exons encode protein domains that are targeted by drugs that selectively inhibit Cav1.3 activity, the alternative splicing events described could also be important for drug discovery and therapeutic intervention. Support or Funding Information National Institute of General Medical Sciences Grant 1R15GM119099‐01 This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .