| First Author | Hulme JT | Year | 2002 |
| Journal | J Biol Chem | Volume | 277 |
| Issue | 6 | Pages | 4079-87 |
| PubMed ID | 11733497 | Mgi Jnum | J:74535 |
| Mgi Id | MGI:2158594 | Doi | 10.1074/jbc.M109814200 |
| Citation | Hulme JT, et al. (2002) A novel leucine zipper targets AKAP15 and cyclic AMP-dependent protein kinase to the C terminus of the skeletal muscle Ca2+ channel and modulates its function. J Biol Chem 277(6):4079-87 |
| abstractText | In skeletal muscle, voltage-dependent potentiation of L-type Ca(2+) channel (Ca(V)1.1) activity requires phosphorylation by cyclic AMP-dependent protein kinase (PKA) anchored via an A kinase-anchoring protein (AKAP15). However, the mechanism by which AKAP15 targets PKA to L-type Ca(2+) channels has not been elucidated. Here we report that AKAP15 directly interacts with the C-terminal domain of the alpha(1) subunit of Ca(V)1.1 via a leucine zipper (LZ) motif. Disruption of the LZ interaction effectively inhibits voltage-dependent potentiation of L-type Ca(2+) channels in skeletal muscle cells. Our results reveal a novel mechanism whereby anchoring of PKA to Ca(2+) channels via LZ interactions ensures rapid and efficient phosphorylation of Ca(2+) channels in response to local signals such as cAMP and depolarization. |
