Role of CFTR’s intrinsic adenylate kinase activity in gating of the Cl− channel

Christoph Randak; Michael Welsh

doi:10.1007/s10863-007-9119-5

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Role of CFTR’s intrinsic adenylate kinase activity in gating of the Cl− channel

Journal article

Peer reviewed

Role of CFTR’s intrinsic adenylate kinase activity in gating of the Cl− channel

Christoph Randak and Michael Welsh

Journal of bioenergetics and biomembranes, Vol.39(5), pp.473-479

12/2007

DOI: 10.1007/s10863-007-9119-5

PMID: 17965924

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Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) is a Cl−channel in the ATP-binding cassette (ABC) transporter protein family. CFTR features the modular design characteristic of ABC transporters, which includes two membrane-spanning domains forming the channel pore, and two ABC nucleotide-binding domains that interact with ATP and contain the enzymatic activity coupled to normal gating. Like other ABC transporters CFTR is an ATPase (ATP + H2O → ADP + Pi). Recent work has shown that CFTR also possesses intrinsic adenylate kinase activity (ATP + AMP ⇆ ADP + ADP). This finding raises important questions: How does AMP influence CFTR gating? Why does ADP inhibit CFTR current? Which enzymatic activity gates CFTR in vivo? Are there implications for other ABC transporters? This minireview attempts to shed light on these questions by summarizing recent advances in our understanding of the role of the CFTR adenylate kinase activity for channel gating.

Biochemistry, general

AMP

Animal Biochemistry

ATPase

Cystic fibrosis

ADP

Bioorganic Chemistry

NBD

Chemistry

Adenylate kinase

Nucleotide binding

Chloride channel

Animal Anatomy / Morphology / Histology

ABC transporter

CFTR

Organic Chemistry

Details

Title: Subtitle: Role of CFTR’s intrinsic adenylate kinase activity in gating of the Cl− channel
Creators: Christoph Randak - Department of Pediatrics Roy J. and Lucille A. Carver College of Medicine, University of Iowa 500 EMRB Iowa IA 52242 USA
Michael Welsh - Department of Internal Medicine, Physiology and Biophysics Howard Hughes Medical Institute, University of Iowa 500 EMRB Iowa IA 52242 USA
Resource Type: Journal article
Publication Details: Journal of bioenergetics and biomembranes, Vol.39(5), pp.473-479
Publisher: Springer US
DOI: 10.1007/s10863-007-9119-5
PMID: 17965924
ISSN: 0145-479X
eISSN: 1573-6881
Language: English
Date published: 12/2007
Academic Unit: Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Pulmonary Medicine; Stead Family Department of Pediatrics; Fraternal Order of Eagles Diabetes Research Center; Neurosurgery; Internal Medicine
Record Identifier: 9984093341402771

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