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."
rlimsp
"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."