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ATP5O — ATPIF1

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• MIPS CORUM F1F0-ATP synthase (EC 3.6.3.14), mitochondrial: F1F0-ATP synthase (EC 3.6.3.14), mitochondrial complex (ATP5A1-ATP5B-ATP5C1-ATP5D-ATP5E-ATP5F1-ATP5G1-ATP5H-ATP5I-ATP5J-ATP5J2-ATP5L-ATP5O-ATPIF1-MT-ATP6-MT-ATP8) Aggeler et al., J Biol Chem 2002
• IRef Corum Interaction: Complex of 33 proteins (association, coimmunoprecipitation) Aggeler et al., J Biol Chem 2002

Text-mined interactions from Literome

Green et al., Biochim Biophys Acta 2000 (Mitochondrial Myopathies...) : The apparent mechanism of IF(1) inhibition of F ( 1 ) F ( 0 ) -ATPase activity and the biophysical conditions that influence IF(1) activity are summarized
Galkin et al., Eur J Biochem 2004 : Functional transitions of F0F1-ATPase mediated by the inhibitory peptide IF1 in yeast coupled submitochondrial particles ... The mechanism of inhibition of yeast F ( 0 ) F ( 1 ) -ATPase by its naturally occurring protein inhibitor ( IF1 ) was investigated in submitochondrial particles by studying the IF1 mediated ATPase inhibition in the presence and absence of a protonmotive force
García et al., Biochemistry 2006 (Liver Neoplasms, Experimental) : Removal of IF1 from rat liver or bovine heart submitochondrial particles increased the F1F0-ATPase activity and decreased the D/M ratio of the ATP synthase
Campanella et al., Trends Biochem Sci 2009 : Although this activity can deplete ATP and precipitate cell death, it is limited by the mitochondrial protein IF(1) , an endogenous F ( 1 ) F ( o ) -ATPase inhibitor
Galante et al., Biochemistry 1981 : This indicates that the active state of the enzyme is necessary for the IF1 effect to be manifested, because F1-ATPase , which does not contain nor require phospholipids for catalyzing ATP hydrolysis, can be inhibited by IF1 plus ATP-Mg2+ in the absence of added phospholipids ... Under conditions that IF1 caused approximately 75 % inhibition of ATPase activity of complex V, no more than 10 % of the ATP-Pi exchange activity was inhibited
Klein et al., Biochemistry 1981 : Adenylyl imidodiphosphate and quercetin, two compounds which partially mimic the inhibitory effect of IF1 on ATPase activity of F1, markedly prevented the binding of ( 14C ) MABI-IF1 to F1 ; on the other hand, aurovertin, a specific ligand of the beta subunit of F1, did not affect the interaction between ( 14C ) MABI-IF1 and F1
Lopez-Mediavilla et al., Eur J Biochem 1993 : Monoclonal antibodies reacting with the inhibitor protein ( IF1 ) of the mitochondrial ATPase/ATP synthase complex did not modify the IF1 induced inhibition of soluble F1 ATPase activity
Rouslin et al., J Bioenerg Biomembr 1993 (Myocardial Ischemia) : Addition of Zn2+ after the formation of fully inhibited IF1-ATPase complexes very slowly reversed IF1 mediated ATPase inhibition without causing significant IF1 release from the membranes
Rouslin et al., Arch Biochem Biophys 1993 : We examined the effects of a variety of conditions upon the IF1 mediated inhibition of the ATPase in both intact and sonicated mitochondria and in IF1 depleted submitochondrial particles ( SMP ) in species-homologous and species-heterologous combinations of IF1 and ATPase ... IF1 mediated ATPase inhibition occurred in intact rabbit heart mitochondria at low matrix pH and low membrane potential, but not in intact pigeon and rat heart mitochondria under the same conditions ... IF1 mediated ATPase inhibition was, however, demonstrable in both the rabbit and pigeon heart systems in sonicated mitochondria incubated at low ionic strength ... The rat heart system failed to exhibit significant IF1 mediated ATPase inhibition in either intact or sonicated mitochondria due to the low amount of IF1 present ... When rabbit heart IF1 containing extracts were incubated with IF1 depleted rabbit heart SMP over a range of KCl concentrations, increasing the [ KCl ] to 100 mM had little effect on IF1 mediated ATPase inhibition ... When pigeon heart IF1 containing extracts were incubated with IF1 depleted pigeon heart SMP under the same conditions, increasing [ KCl ] to 100 mM nearly completely blocked IF1 mediated ATPase inhibition ... When rabbit, pigeon, or rat heart IF1 was bound to rabbit versus pigeon IF1 depleted SMP, the effect of varying ionic strength on IF1 mediated ATPase inhibition was related to the species source of the IF1, not to the species source of the enzyme ; 1x bovine heart IF1 purified to homogeneity behaved much like 1x crude rabbit heart IF1 when binding to either the rabbit or the pigeon heart enzyme
Rouslin et al., Biochem Biophys Res Commun 1996 : In such slow heart-rate mammalian species, it completely prevents IF1 mediated ATPase inhibition regardless of pH while concomitantly causing full IF1 binding to the ATPase, again, regardless of pH ( Rouslin et al. ( 1993 ) J. Bioenerget ... In the present study we show that, in contrast to its effects in rabbit cardiomyocytes, mitochondria, and SMP in which Zn2+ fully blocked IF1 mediated ATPase inhibition, Zn2+ actually enhanced ATPase inhibition in rat cardiomyocytes, although the extent of this effect was limited by the low level of IF1 in rat cardiomyocytes ... Moreover, Zn2+ had no effect on IF1 mediated ATPase inhibition in rat heart mitochondria and, as suggested by inter and intra-species IF1 binding to SMP, the different effects of Zn2+ in rabbit versus those in rat appear to be mediated primarily through the different reactivities of rabbit and rat IF1 to Zn2+