IndraLab

Statements

PKA phosphorylates KCNQ1 on S27. 14 / 14
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"PKA phosphorylates Ser27 on KCNQ1 to modulate I Ks and phosphorylates Ser43 of Yotiao to further enhance regulation by the sympathetic nervous system, whereas dephosphorylation of these sites and suppression of I Ks currents are facilitated by anchored PP1 ( xref – xref )."
23043438
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"Stimulation of beta-adrenergic receptors increases the magnitude of I Ks in the heart via a protein kinase A (PKA)-dependent phosphorylation of Ser 27 of KCNQ1 [83]."
12623297
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"Upon β-AR stimulation, Yotiao-anchored PKA phosphorylates KCNQ1 at Ser27, increasing I Ks , which shortens the action potential duration to maintain diastolic time intervals [ xref ]."
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"The primary function of the AKAP9 bound PKA is to phosphorylate the S27 residue on KCNQ1."
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"Stimulation of β-adrenergic receptors increases the magnitude of I Ks in the heart via a protein kinase A (PKA)-dependent phosphorylation of Ser-27 of KCNQ1 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"KCNQ1-KCNE3 complexes do not show the same upregulation in response to PKA phosphorylation of KCNQ1 S27 ( Kurokawa et al., 2009 )."
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"KCNQ1-KCNE3 complexes do not show the same upregulation in response to PKA phosphorylation of KCNQ1 S27 59."
26410412
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"We find cAMP mediated PKA phosphorylation of KCNQ1 (at residue Ser 27) is not affected by its expression with the KCNE variants KCNE1, KCNE2 or KCNE3."
19077539
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"KCNQ1-KCNE3 complexes do not show the same upregulation in response to PKA phosphorylation of KCNQ1 S27 (Kurokawa et al., 2009)."
26410412
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"β-adrenergic regulation of I Ks is mediated by a macromolecular signaling complex consisting of KCNQ1, KCNE1 and Yotiao (an AKAP) that regulates channel activity by PKA-dependent phosphorylation of Ser 27 in the N-terminal KCNQ1 ( xref ), and of Ser 43 in the N-terminal of Yotiao ( xref , xref )."
23242028
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"PKA phosphorylates Ser27 on KCNQ1 to modulate I Ks and phosphorylates Ser43 of Yotiao to further enhance regulation by the sympathetic nervous system, whereas dephosphorylation of these sites and suppression of I Ks currents are facilitated by anchored PP1."
23043438
reach
"beta-adrenergic regulation of I Ks is mediated by a macromolecular signaling complex consisting of KCNQ1, KCNE1 and Yotiao (an AKAP) that regulates channel activity by PKA dependent phosphorylation of Ser 27 in the N-terminal KCNQ1, and of Ser 43 in the N-terminal of Yotiao."
23242028
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"Initial studies show that PKA can mediated phosphorylation of KCNQ1 at position Ser27 at its C-terminal tail, which may by counteracted by PP1 and regulated by the accessory protein Yotiao."
26617522
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"XREF_BIBR, XREF_BIBR To mimic PKA phosphorylation of KCNQ1, we replaced KCNQ1 Ser 27 by Asp (S27D) to change the charge at this residue and refer to the construct as pseudo phosphorylated KCNQ1 as we have previously reported."
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