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PMID: 21455600
Siwiak M, Edelman A, Zielenkiewicz P
Structural models of CFTR-AMPK and CFTR-PKA interactions: R-domain flexibility is a key factor in CFTR regulation.
J Mol Model. 2011 Apr 1., 2011-04-01
[PubMed]
Sentences
No.
Mutations
Sentence
Comment
121
ABCC7 p.Ser737Ala
X
ABCC7 p.Ser737Ala 21455600:121:103
status:
NEW
view ABCC7 p.Ser737Ala details
ABCC7 p.Ser768Ala
X
ABCC7 p.Ser768Ala 21455600:121:109
status:
NEW
view ABCC7 p.Ser768Ala details
However, experiments [7] have shown an 80% decrease in AMPK phosphorylation for the CFTR double mutant
S737A
-
S768A
.
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155
ABCC7 p.Ser737Ala
X
ABCC7 p.Ser737Ala 21455600:155:152
status:
NEW
view ABCC7 p.Ser737Ala details
ABCC7 p.Ser768Ala
X
ABCC7 p.Ser768Ala 21455600:155:158
status:
NEW
view ABCC7 p.Ser768Ala details
This shows that, at the molecular level, it is possible that 20% of the currently unexplained phosphorylation signal observed in the CFTR double mutant
S737A
-
S768A
incubated with AMPK may come from "activator" serines such as S813.
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156
ABCC7 p.Ser737Ala
X
ABCC7 p.Ser737Ala 21455600:156:152
status:
NEW
view ABCC7 p.Ser737Ala details
ABCC7 p.Ser768Ala
X
ABCC7 p.Ser768Ala 21455600:156:158
status:
NEW
view ABCC7 p.Ser768Ala details
This shows that, at the molecular level, it is possible that 20% of the currently unexplained phosphorylation signal observed in the CFTR double mutant
S737A
-
S768A
incubated with AMPK may come from "activator" serines such as S813.
Login to comment