被撤回的出版物: L-type Ca2+ channel facilitation mediated by phosphorylation of the β subunit by CaMKII (Retracted article. See vol. 58, pg. 388, 2015)

L-type Ca2+ channels (LTCCs) are major entry points for Ca2+ in many cells. Ca2+/calmodulin-dependent protein kinase II (CaMKII) is associated with cardiac LTCC complexes and increases channel open probability (P-O) to dynamically increase Ca2+ current (I-Ca) and augment cellular Ca2+ signaling by a process called facilitation. However, the critical molecular mechanisms for CaMKII localization to LTCCs and I-Ca facilitation in cardiomyocytes have not been defined. We show CaMKII binds to the LTCC beta(2a) subunit and preferentially phosphorylates Thr498 in beta(2a). Mutation of Thr498 to Ala (T498A) in beta(2a) prevents CaMKII-mediated increases in the P-O of recombinant LTCCs. Moreover, expression of beta(2a).(T498A) in adult cardiomyocytes ablates CaMKII-mediated I-Ca facilitation, demonstrating that phosphorylation of beta(2a) at Thr498 modulates native calcium channels. These findings reveal a molecular mechanism for targeting CaMKII to LTCCs and facilitating I-Ca that may modulate Ca2+ entry in diverse cell types coexpressing CaMKII and the beta(2a) subunit.