Shedding light on molecular mechanisms and identity of mPTP

Mitochondrion

Volumn 21, Issue , 2015, Pages 11-

  Bonora, Massimo ^a   Pinton, Paolo ^a  

^a UNIVERSITY OF FERRARA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; CYCLOPHILIN D; CYCLOSPORIN A; MAGNESIUM ION; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PHOSPHATE; PROTEIN BCL XL; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; MULTIPROTEIN COMPLEX;

BILAYER MEMBRANE; CATALYSIS; LETTER; MITOCHONDRIAL PERMEABILITY; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STOICHIOMETRY; ENZYMOLOGY; METABOLISM;

MITOCHONDRIA; MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES; MULTIPROTEIN COMPLEXES;

EID: 84936943453     PISSN: 15677249     EISSN: 18728278     Source Type: Journal    
DOI: 10.1016/j.mito.2014.10.001     Document Type: Letter

References (8)

1. Alavian K.N., Li H., Collis L., Bonanni L., Zeng L., Sacchetti S., Lazrove E., Nabili P., Flaherty B., Graham M., Chen Y., Messerli S.M., Mariggio M.A., Rahner C., McNay E., Shore G.C., Smith P.J.S., Hardwick J.M., Jonas E.A. Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase. Nat. Cell Biol. 2011, 13:1224-1233. 10.1038/ncb2330.
2. Alavian K.N., Beutner G., Lazrove E., Sacchetti S., Park H.-A., Licznerski P., Li H., Nabili P., Hockensmith K., Graham M., Porter G.A., Jonas E.A. An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore. Proc. Natl. Acad. Sci. U. S. A. 2014, (1401591111). 10.1073/pnas.1401591111.
3. Azarashvili T., Odinokova I., Bakunts A., Ternovsky V., Krestinina O., Tyynelä J., Saris N.-E.L. Potential role of subunit c of F0F1-ATPase and subunit c of storage body in the mitochondrial permeability transition. Effect of the phosphorylation status of subunit c on pore opening. Cell Calcium 2014, 55:69-77. 10.1016/j.ceca.2013.12.002.
4. Bonora M., Bononi A., De Marchi E., Giorgi C., Lebiedzinska M., Marchi S., Patergnani S., Rimessi A., Suski J.M., Wojtala A., Wieckowski M.R., Kroemer G., Galluzzi L., Pinton P. Role of the c subunit of the FO ATP synthase in mitochondrial permeability transition. Cell Cycle 2013, 12:674-683. 10.4161/cc.23599.
5. De Marchi E., Bonora M., Giorgi C., Pinton P. The mitochondrial permeability transition pore is a dispensable element for mitochondrial calcium efflux. Cell Calcium 2014, 56:1-13. 10.1016/j.ceca.2014.03.004.
6. Giorgio V., Bisetto E., Soriano M.E., Dabbeni-Sala F., Basso E., Petronilli V., Forte M.a, Bernardi P., Lippe G. Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex. J. Biol. Chem. 2009, 284:33982-33988. 10.1074/jbc.M109.020115.
7. McGeoch J.E., Palmer D.N. Ion pores made of mitochondrial ATP synthase subunit c in the neuronal plasma membrane and Batten disease. Mol. Genet. Metab. 1999, 66:387-392. 10.1006/mgme.1999.2822.
8. Pogoryelov D., Reichen C., Klyszejko A.L., Brunisholz R., Muller D.J., Dimroth P., Meier T. The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15. J. Bacteriol. 2007, 189:5895-5902. 10.1128/JB.00581-07.