
IndraLab
Statements
sparser
"Maximal PKA phosphorylation of Cav1.2 and RyR2 is reduced inCacna1c +/− compared to WT myocytes, leaving “empty”, i.e., non-phosphorylated serine residues (S1928 and S2808) in Cav1.2 and RyR2 (see white circles) and suggesting—once again—altered local regulation of cAMP and PKA-dependent phosphorylation in the dyadic cleft ofCacna1c +/− myocytes."
sparser
"Some of the cardinal debated issues include details of specific subunits and residues in CaV1.2 phosphorylated by PKA, the nature, extent, and role of post-translational processing of CaV1.2, and the role of auxiliary proteins (such as A kinase anchoring proteins) involved in PKA regulation."
reach
"Although the two phenomena occur simultaneously during physiological exercise, we separated them to dissect their relative contributions.Activation of β-adrenergic receptors is known to lead to an increase of both L-Type Ca current (I ) and slow delayed rectifier I , via protein kinase A (PKA)-mediated phosphorylation of Cav1.2 and Kv7.1 channels, respectively."
sparser
"Although phosphorylation of Cav1.2-pS1928 is not required for β-adrenoceptor stimulation of LTCC in mouse ventricular myocytes and HEK293 cells, xref it is a well-established Cav1.2 PKA phosphorylation site xref and phosphorylation of its α 1C subunit is relevant for channel function by increasing trafficking to the plasma membrane. xref In CON, the relative Cav1.2-pS1928 phosphorylation was significantly lower in cAF compared to SR and increased significantly after incubation with ISO or PF to levels seen in corresponding CONs ( xref and xref , xref ), pointing to significant contribution of PDE8 to LTCC dephosphorylation."