IF1: setting the pace of the F1Fo-ATP synthase

Trends in Biochemical Sciences

Volumn 34, Issue 7, 2009, Pages 343-350

  Campanella, Michelangelo ^a,b   Parker, Nadeene ^a   Tan, Choon Hong ^a   Hall, Andrew M ^a   Duchen, Michael R ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b ROYAL VETERINARY COLLEGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HYDROLASE; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; PROTEIN IF1; PROTEIN SUBUNIT; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; APOPTOSIS; CYTOLOGY; DISEASE COURSE; DISORDERS OF MITOCHONDRIAL FUNCTIONS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE; GENE MUTATION; GENETIC DISORDER; GLYCOLYSIS; HUMAN; HYDROLYSIS; HYPOXIA; ISCHEMIA; MITOCHONDRIAL MEMBRANE POTENTIAL; MITOCHONDRIAL RESPIRATION; MOTOR NEURON DISEASE; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RESPIRATORY CHAIN; REVIEW; SIGNAL TRANSDUCTION;

ADENOSINE TRIPHOSPHATE; ANIMALS; ENERGY METABOLISM; HUMANS; MEMBRANE POTENTIAL, MITOCHONDRIAL; MITOCHONDRIA; MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES; PROTEINS;

EID: 67649948810     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2009.03.006     Document Type: Review

References (42)

1. Rich P. Chemiosmotic coupling: The cost of living. Nature 421 (2003) 583
2. 2+ signalling. Physiology (Bethesda) 23 (2008) 84-94
3. 2+ in cell physiology and pathophysiology. Cell Calcium 28 (2000) 339-348
4. Kroemer G., et al. Mitochondrial control of apoptosis. Immunol. Today 18 (1997) 44-51
5. Duchen M.R. Mitochondria in health and disease: perspectives on a new mitochondrial biology. Mol. Aspects Med. 25 (2004) 365-451
6. Irwin W.A., et al. Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency. Nat. Genet. 35 (2003) 367-371
7. Affourtit C., et al. Novel uncoupling proteins. Novartis Found. Symp. 287 (2007) 70-80
8. Boyer P.D. The ATP synthase-a splendid molecular machine. Annu. Rev. Biochem. 66 (1997) 717-749
9. Walker J.E., et al. ATP synthase from bovine mitochondria: sequences of imported precursors of oligomycin sensitivity conferral protein, factor 6, and adenosinetriphosphatase inhibitor protein. Biochemistry 26 (1987) 8613-8619
10. Krebs H.A. The Pasteur effect and the relations between respiration and fermentation. Essays Biochem. 8 (1972) 1-34
11. David G., and Nicholls S.J.F. Bioenergetics (2002), Academic Press
12. McKenzie M., et al. Mitochondrial ND5 gene variation associated with encephalomyopathy and mitochondrial ATP consumption. J. Biol. Chem. 282 (2007) 36845-36852
13. Allue I., et al. Evidence for rapid consumption of millimolar concentrations of cytoplasmic ATP during rigor-contracture of metabolically compromised single cardiomyocytes. Biochem. J. 319 (1996) 463-469
14. 2+]i studied in isolated rat cardiomyocytes. J. Physiol. 496 (1996) 111-128
15. 0-ATPase: effect of selective pharmacological inhibition of mitochondrial ATPase hydrolase activity. Am. J. Physiol. Heart Circ. Physiol. 287 (2004) H1747-H1755
16. In: Jacobson M.D., and McCarthy N. (Eds). Apoptosis: The Molecular Biology of Programmed Cell Death (2002), Oxford University Press
17. Pullman M.E., and Monroy G.C. A naturally occurring inhibitor of mitochondrial adenosine triphosphatase. J. Biol. Chem. 238 (1963) 3762-3769
18. Rouslin W., and Pullman M.E. Protonic inhibition of the mitochondrial adenosine 5′-triphosphatase in ischemic cardiac muscle. Reversible binding of the ATPase inhibitor protein to the mitochondrial ATPase during ischemia. J. Mol. Cell. Cardiol. 19 (1987) 661-668
19. Gledhill J.R., et al. How the regulatory protein, IF1, inhibits F1-ATPase from bovine mitochondria. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 15671-15676
20. Rouslin W., et al. ATPase activity, IF1 content, and proton conductivity of ESMP from control and ischemic slow and fast heart-rate hearts. J. Bioenerg. Biomembr. 27 (1995) 459-466
21. 1ATPsynthase and calmodulin. J. Bioenerg. Biomembr. 39 (2007) 291-300
22. 1 ATP synthase inhibitor protein. J. Bioenerg. Biomembr. 37 (2005) 317-326
23. Rouslin W. Protonic inhibition of the mitochondrial oligomycin-sensitive adenosine 5′-triphosphatase in ischemic and autolyzing cardiac muscle. Possible mechanism for the mitigation of ATP hydrolysis under nonenergizing conditions. J. Biol. Chem. 258 (1983) 9657-9661
24. Tuena Gomez-Puyou M.T., et al. Synthesis and hydrolysis of ATP by the mitochondrial ATP synthase. Biochem. Cell Biol. 66 (1988) 677-682
25. Cabezon E., et al. The structure of bovine F1-ATPase in complex with its regulatory protein IF1. Nat. Struct. Biol. 10 (2003) 744-750
26. 0-ATP synthase. Biochemistry 45 (2006) 12695-12703
27. Buzhynskyy N., et al. Rows of ATP synthase dimers in native mitochondrial inner membranes. Biophys. J. 93 (2007) 2870-2876
28. Wittig I., et al. Characterization of domain interfaces in monomeric and dimeric ATP synthase. Mol. Cell. Proteomics 7 (2008) 995-1004
29. 1ATP synthase from bovine heart is independent from the binding of the inhibitor protein IF1. Biochim. Biophys. Acta 1556 (2002) 133-141
30. o-ATPase inhibitor protein, IF1. Cell Metab. 8 (2008) 13-25
31. Hall A.M., et al. Multiphoton imaging reveals differences in mitochondrial function between nephron segments. J. Am. Soc. Nephrol. 20 (2009) 1293-1302
32. Bagnasco S., et al. Lactate production in isolated segments of the rat nephron. Am. J. Physiol. 248 (1985) F522-F526
33. Magistretti P.J. Neuron-glia metabolic coupling and plasticity. J. Exp. Biol. 209 (2006) 2304-2311
34. Niaudet P., and Rotig A. The kidney in mitochondrial cytopathies. Kidney Int. 51 (1997) 1000-1007
35. Huang L.J., et al. Suppression of mitochondrial ATPase inhibitor protein (IF1) in the liver of late septic rats. Biochim. Biophys. Acta 1767 (2007) 888-896
36. Huang L.-J., and Yang R.-C. Hypoxia-inducible factor-1α regulates the hepatic mitochondrial ATPase inhibitory protein (IF1) [abstract]. FASEB J. 22 (2008) 1190.13
37. Shen, L. et al. (2008) IEX-1 targets mitochondrial F1Fo-ATPase inhibitor for degradation. Cell Death. Differ. DOI:10.1038/ cdd.2008.184.
38. 0-ATPase. Biochim. Biophys. Acta 1458 (2000) 343-355
39. Strauss M., et al. Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J. 27 (2008) 1154-1160
40. Allen R.D., et al. An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques. J. Cell Biol. 108 (1989) 2233-2240
41. Giraud M.F., et al. Is there a relationship between the supramolecular organization of the mitochondrial ATP synthase and the formation of cristae?. Biochim. Biophys. Acta 1555 (2002) 174-180
42. Minauro-Sanmiguel F., et al. Structure of dimeric mitochondrial ATP synthase: novel F0 bridging features and the structural basis of mitochondrial cristae biogenesis. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 12356-12358