Journal article
Binding of the proline-rich region of the epithelial Na+ channel to SH3 domains and its association with specific cellular proteins
Biochemical journal, Vol.312(2), pp.491-497
12/01/1995
DOI: 10.1042/bj3120491
PMCID: PMC1136289
PMID: 8526861
Abstract
The amiloride-sensitive epithelial Na+ channel (ENaC) is an important component of the Na(+)-reabsorption pathway in many epithelia. The identification of three subunits of ENaC (alpha, beta and gamma), as well as results from a number of functional and biochemical studies, suggests that functional Na+ channels are composed of a complex of proteins. To learn about possible interactions of the channel with other proteins, we studied the alpha-subunit of rat and human ENaC. We found that the proline-rich C-terminal domains of both rat and human alpha-ENaC, expressed as glutathione S-transferase fusion proteins, bound to SH3 domains in vitro. A 116 kDa protein from a human lung adenocarcinoma cell line (H441) was specifically bound by the human alpha-ENaC C-terminal fusion protein and by a shorter 18-amino acid proline-rich peptide derived from the larger fusion protein. The 116 kDa protein was not glycosylated and was not phosphorylated on tyrosine or by cyclic AMP-dependent protein kinase (PKA). A 134 kDa protein which was also bound by the human alpha-ENaC C-terminal fusion protein was a substrate for phosphorylation by PKA. These data suggest that the proline-rich C-terminal tail of alpha-ENaC may interact with other proteins that control its function, regulation or localization.
Details
- Title: Subtitle
- Binding of the proline-rich region of the epithelial Na+ channel to SH3 domains and its association with specific cellular proteins
- Creators
- F J McDonald - Howard Hughes Medical Institute, Department of Internal Medicine, Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242, U.S.AM J Welsh - Howard Hughes Medical Institute, Department of Internal Medicine, Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242, U.S.A
- Resource Type
- Journal article
- Publication Details
- Biochemical journal, Vol.312(2), pp.491-497
- DOI
- 10.1042/bj3120491
- PMID
- 8526861
- PMCID
- PMC1136289
- ISSN
- 0264-6021
- eISSN
- 1470-8728
- Language
- English
- Date published
- 12/01/1995
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Fraternal Order of Eagles Diabetes Research Center; Neurosurgery; Internal Medicine
- Record Identifier
- 9984020706002771
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