| First Author | Lemke T | Year | 2008 |
| Journal | J Biol Chem | Volume | 283 |
| Issue | 50 | Pages | 34738-44 |
| PubMed ID | 18829456 | Mgi Jnum | J:143613 |
| Mgi Id | MGI:3828241 | Doi | 10.1074/jbc.M804981200 |
| Citation | Lemke T, et al. (2008) Unchanged beta-adrenergic stimulation of cardiac L-type calcium channels in Ca v 1.2 phosphorylation site S1928A mutant mice. J Biol Chem 283(50):34738-44 |
| abstractText | Phosphorylation of serine 1928 (Ser(1928)) of the cardiac Ca(v)1.2 subunit of L-type Ca(2+) channels has been proposed as the mechanism for regulation of L-type Ca(2+) channels by protein kinase A (PKA). To test this directly in vivo, we generated a knock-in mouse with targeted mutation of Ser(1928) to alanine. This mutation did not affect basal L-type current characteristics or regulation of the L-type current by PKA and the beta-adrenergic receptor, whereas the mutation abolished phosphorylation of Ca(v)1.2 by PKA. Therefore, our data show that PKA phosphorylation of Ser(1928) of Ca(v)1.2 is not functionally involved in beta-adrenergic stimulation of Ca(v)1.2-mediated Ca(2+) influx into the cardiomyocyte. |
