Ca2+-modulated phosphorylation of a low-molecular-mass polypeptide in rat liver mitochondria: Evidence that it is identical with subunit c of F0F1-ATPase

Authors
Azarashvily, TS Tyynela, J Baumann, M Evtodienko, YV Saris, NEL
Citation
Ts. Azarashvily et al., Ca2+-modulated phosphorylation of a low-molecular-mass polypeptide in rat liver mitochondria: Evidence that it is identical with subunit c of F0F1-ATPase, BIOC BIOP R, 270(3), 2000, pp. 741-744
Citations number
31
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
270
Issue
3
Year of publication
2000
Pages
741 - 744
Database
ISI
SICI code
0006-291X(20000421)270:3<741:CPOALP>2.0.ZU;2-2
Abstract
A 3.5-kDa polypeptide associated with the inner membrane of rat liver was f ound to be phosphorylated by [gamma-P-32]ATP, presumably via a cAMP-depende nt kinase. The phosphorylation was modulated by [Ca2+] in the physiological range, with a minimum at 1 mu M and rising fourfold toward lower (10 nM) a nd higher (10 mu M) concentrations. Further characterization of the 3.5-kDa component showed that the polypeptide has the same electrophoretic mobilit y as subunit c of F0F1-ATPase and that it selectively binds to antibodies a gainst subunit c. (C) 2000 Academic Press.