Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 이경림 | * |
dc.contributor.author | 윤태숙 | * |
dc.date.accessioned | 2016-08-28T11:08:09Z | - |
dc.date.available | 2016-08-28T11:08:09Z | - |
dc.date.issued | 2002 | * |
dc.identifier.issn | 0021-9258 | * |
dc.identifier.other | OAK-1267 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/219106 | - |
dc.description.abstract | We reported previously that cofilin, an actin-binding protein, interacts with Na,K-ATPase and enhances its activity (Lee, K., Jung, J., Kim, M., and Guidotti, G. (2001) Biochem. J. 353, 377-385). To understand the nature of this interaction and the role of cofilin in the regulation of Na,K-ATPase activity, we searched for cofilin-binding proteins in the rat skeletal muscle cDNA library using the yeast two-hybrid system. Several cDNA clones were isolated, some of which coded for triose-phosphate isomerase, a glycolytic enzyme. The interaction of cofilin with triose-phosphate isomerase as well as Na,K-ATPase was confirmed by immunoprecipitation and confocal microscopy in HeLa cells. Cofilin was translocated to the plasma membrane along with triose-phosphate isomerase by the Rho activator lysophosphatidic acid but not by the p160 Rho-associated kinase inhibitor Y-27632, suggesting that the phosphorylated form of cofilin bound to TPI interacts with Na,K-ATPase. Ouahain-sensitive 86Rb + uptake showed that Na,K-ATPase activity was increased by the overexpression of cofilin and lysophosphatidic acid treatment, but not by the overexpression of mutant cofilin S3A and Y-27632 treatment. Pretreatment with the glycolytic inhibitor iodoacetic acid caused a remarkable reduction of Na,K-ATPase activity, whereas pretreatment with the oxidative inhibitor carhonyl cyanide m-chlorophenylhydrazone caused no detectable changes, suggesting that the phosphorylated cofilin is involved in feeding glycolytic fuel for Na,K-ATPase activity. These findings provide a novel molecular mechanism for the regulation of Na,K-ATPase activity and for the nature of the functional coupling of cellular energy transduction. | * |
dc.language | English | * |
dc.title | Interaction of cofilin with triose-phosphate isomerase contributes glycolytic fuel for Na,K-ATPase via Rho-mediated signaling pathway | * |
dc.type | Article | * |
dc.relation.issue | 50 | * |
dc.relation.volume | 277 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 48931 | * |
dc.relation.lastpage | 48937 | * |
dc.relation.journaltitle | Journal of Biological Chemistry | * |
dc.identifier.doi | 10.1074/jbc.M208806200 | * |
dc.identifier.wosid | WOS:000179789600124 | * |
dc.identifier.scopusid | 2-s2.0-0037073759 | * |
dc.author.google | Jung J. | * |
dc.author.google | Yoon T. | * |
dc.author.google | Choi E.C. | * |
dc.author.google | Lee K. | * |
dc.contributor.scopusid | 이경림(7501517435) | * |
dc.contributor.scopusid | 윤태숙(7201604364) | * |
dc.date.modifydate | 20240301081003 | * |