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. Login to comment
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. Login to comment
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