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Interaction of the α subunit of Na,K-ATPase with, cofilin

Title
Interaction of the α subunit of Na,K-ATPase with, cofilin
Authors
Lee K.Jung J.Kim M.Guidotti G.
Ewha Authors
이경림
SCOPUS Author ID
이경림scopus
Issue Date
2001
Journal Title
Biochemical Journal
ISSN
0264-6021JCR Link
Citation
vol. 353, no. 2, pp. 377 - 385
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The α1 subunit of rat Na,K-ATPase, composed of 1018 amino acids, is arranged in the membrane so that the middle third of the polypeptide forms a large cytoplasmic loop bordered on both sides by multiple transmembrane segments. To identify proteins that might interact with the large cytoplasmic loop of Na,K-ATPase and potentially affect the function and/or the disposition of the pump in the cell, the yeast two-hybrid system was used to screen a rat skeletal muscle cDNA library. Several cDNA clones were isolated, some of which coded for cofilin, an actin-binding protein. Cofilin was co-immunoprecipitated with the α subunit of Na,K-ATPase from extracts of COS-7 cells transiently transfected with haemagglutinin-epitope-tagged cofilin cDNA as well as from yeast extracts. By means of deletion analysis we showed that the segment of cofilin between residues 45 and 99 is essential for functional association with the large cytoplasmic loop of Na,K-ATPase. Recombinant cofilin was shown to bind to the membrane-bound Na,K-ATPase; the association between the two proteins was demonstrated by confocal microscopy. The increased level of cofilin in transfected COS-7 cells caused an increase in the rate of ouabain-sensitive 86Rb+ uptake, indicating that cofilin elicits, either directly or indirectly, enhanced Na,K-ATPase activity and that the interaction occurs in vivo.
DOI
10.1042/0264-6021:3530377
Appears in Collections:
약학대학 > 약학과 > Journal papers
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