AKAP5 Keeps L-type Channels and NFAT on Their Toes

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AKAP5 Keeps L-type Channels and NFAT on Their Toes Manuel F. Navedo, Johannes W. Hell Cell Reports Volume 7, Issue 5, Pages 1341-1342 (June 2014) DOI: 10.1016/j.celrep.2014.05.052 Copyright © 2014 The Authors Terms and Conditions

Figure 1 The Cav1.2/PKA/CaN/NFAT Signaling Complex AKAP5 interacts with the N terminus, loop between domains I and II, and distal C terminus (dark blue bars) of Cav1.2 (Hall et al., 2007; Oliveria et al., 2007). AKAP5-anchored PKA phosphorylates Cav1.2 on S1700 and S1928 in order to augment channel activity. AKAP5-anchored CaN readily dephosphorylates pS1928 (but not pS1700) and NFAT for nuclear translocation. Calmodulin (CaM) preassociates with the IQ motif of Cav1.2 for CDI either via a conformational change or by activating CaN for acute dephosphorylation of Cav1.2. In either case, PKA and CaN affect CDI in an opposing and permissive manner, respectively. Cell Reports 2014 7, 1341-1342DOI: (10.1016/j.celrep.2014.05.052) Copyright © 2014 The Authors Terms and Conditions