{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T18:31:35Z","timestamp":1761676295531},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1995,12,1]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1042\/bj3120491","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:46:20Z","timestamp":1439243180000},"page":"491-497","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Binding of the proline-rich region of the epithelial Na+ channel to SH3 domains and its association with specific cellular proteins"],"prefix":"10.1042","volume":"312","author":[{"given":"F J","family":"McDonald","sequence":"first","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Internal Medicine, Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M J","family":"Welsh","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Internal Medicine, Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/312\/2\/491\/600677\/bj3120491.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/312\/2\/491\/600677\/bj3120491.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T23:44:20Z","timestamp":1637711060000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/312\/2\/491\/32030\/Binding-of-the-proline-rich-region-of-the"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,12,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1995,12,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3120491","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,12,1]]}}}