ABCC8 p.Ser1571Asp
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 10469651
[PubMed]
Beguin P et al: "PKA-mediated phosphorylation of the human K(ATP) channel: separate roles of Kir6.2 and SUR1 subunit phosphorylation."
No.
Sentence
Comment
67
In contrast, the phosphorylation in the S1571A mutant in response to PKA was completely abolished (Figure 3B, compare lane 4 with 7).
X
ABCC8 p.Ser1571Asp 10469651:67:85
status: NEW68 PKA-mediated phosphorylation of human SUR1 was also abolished by the substitution of serine-1571 with aspartic acid (unpublished data).
X
ABCC8 p.Ser1571Asp 10469651:68:85
status: NEW169 In contrast, no significant change was observed in open probability (0.12 Ϯ 0.06 and 0.09 Ϯ 0.03, for wt Kir6.2/SUR1 and wt Kir6.2/ SUR1 S1571D, respectively, n ϭ 4-7) or channel kinetics (unpublished data) for the SUR1 S1571D mutant, as would be expected if SUR1 is already phosphorylated under basal conditions.
X
ABCC8 p.Ser1571Asp 10469651:169:149
status: NEWX
ABCC8 p.Ser1571Asp 10469651:169:238
status: NEW201 Since the PKA action of each subunit can be mimicked by the Kir6.2 (S372D) or SUR1 (S1571D) mutant, the negative charges carried by both subunits seem to be good candidates for this structural change.
X
ABCC8 p.Ser1571Asp 10469651:201:84
status: NEW168 In contrast, no significant change was observed in open probability (0.12 afe; 0.06 and 0.09 afe; 0.03, for wt Kir6.2/SUR1 and wt Kir6.2/ SUR1 S1571D, respectively, n afd; 4-7) or channel kinetics (unpublished data) for the SUR1 S1571D mutant, as would be expected if SUR1 is already phosphorylated under basal conditions.
X
ABCC8 p.Ser1571Asp 10469651:168:149
status: NEWX
ABCC8 p.Ser1571Asp 10469651:168:238
status: NEW