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EPAC1 activation by cAMP stabilizes CFTR at the membrane by promoting its interaction with NHERF1

Abstract:

Cyclic AMP (cAMP) activates protein kinase A (PKA) but also the guanine nucleotide exchange factor 'exchange protein directly activated by cAMP' (EPAC1; also known as RAPGEF3). Although phosphorylation by PKA is known to regulate CFTR channel gating - the protein defective in cystic fibrosis - the contribution of EPAC1 to CFTR regulation remains largely undefined. Here, we demonstrate that in human airway epithelial cells, cAMP signaling through EPAC1 promotes CFTR stabilization at the plasma...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted manuscript

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Publisher copy:
10.1242/jcs.185629

Authors


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Role:
Author
ORCID:
0000-0002-0828-8630
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Physiology Anatomy and Genetics
Oxford college:
Balliol College
Role:
Author
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Role:
Author
ORCID:
0000-0002-5467-1710
European Respiratory Society More from this funder
Publisher:
Company of Biologists Publisher's website
Journal:
Journal of Cell Science Journal website
Volume:
129
Issue:
13
Pages:
2599-2612
Publication date:
2016-05-20
Acceptance date:
2016-05-17
DOI:
EISSN:
1477-9137
ISSN:
0021-9533
Pubs id:
pubs:622996
URN:
uri:f4748055-77b7-447b-a58a-738ca8edb7f3
UUID:
uuid:f4748055-77b7-447b-a58a-738ca8edb7f3
Local pid:
pubs:622996

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