Stoichiometric expression of mtHsp40 and mtHsp70 modulates mitochondrial morphology and cristae structure via Opa1L cleavage

Molecular Biology of the Cell

Volumn 26, Issue 12, 2015, Pages 2156-2167

  Lee, Byoungchun ^a   Ahn, Younghee ^b   Kang, Sung Myung ^a   Park, Youngjin ^c   Jeon, You Jin ^d   Rho, Jong M ^b   Kim, Sung Woo ^b  

^a UNIVERSITY OF CALGARY   (Canada)

^b UNIVERSITY OF CALGARY   (Canada)

^c School of Medicine   (South Korea)

^d Jeju National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; OPTIC ATROPHY 1 PROTEIN; PROTEIN; PROTEIN DRP1; UNCLASSIFIED DRUG; DNAJA3 PROTEIN, HUMAN; GUANOSINE TRIPHOSPHATASE; HSPA9 PROTEIN, HUMAN; MITOCHONDRIAL PROTEIN; OPA1 PROTEIN, HUMAN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; MITOCHONDRIAL RESPIRATION; MITOCHONDRION; MORPHOLOGY; OXIDATIVE PHOSPHORYLATION; OXYGEN CONSUMPTION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CLEAVAGE; PROTEIN EXPRESSION; PROTEIN FUNCTION; STOICHIOMETRY; WESTERN BLOTTING; GENE EXPRESSION; GENETICS; METABOLISM; MITOCHONDRIAL MEMBRANE; MITOPHAGY; PHYSIOLOGY; PROTEIN DEGRADATION; ULTRASTRUCTURE;

GENE EXPRESSION; GTP PHOSPHOHYDROLASES; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; MITOCHONDRIA; MITOCHONDRIAL DEGRADATION; MITOCHONDRIAL MEMBRANES; MITOCHONDRIAL PROTEINS; PROTEOLYSIS;

EID: 84930908324     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E14-02-0762     Document Type: Article

References (31)

1. Ahn BY, Trinh DLN, Zajchowski LD, Lee B, Elwi A.N., Kim S-W (2010). Tid1 is a new regulator of p53 mitochondrial translocation and apoptosis in cancer. Oncogene 29, 1155-1166.
2. Anand R, Wai T, Baker M.J., Kladt N., Schauss AC, Rugarli E, Langer T. (2014). The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission. J Cell Biol 204, 919-929.
3. Burbulla L.F., Schelling C, Kato H., Rapaport D, Woitalla D, Schiesling C., Schulte C, Sharma M, Illig T., Bauer P. (2010). Dissecting the role of the mitochondrial chaperone mortalin in Parkinson's disease: functional impact of disease-related variants on mitochondrial homeostasis. Hum Mol Genet 19, 4437-4452.
4. Cereghetti GM, Stangherlin A, Martins de BO, Chang CR, Blackstone C, Bernardi P, Scorrano L. (2008). Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria. Proc Natl Acad Sci USA 105, 15803-15808.
5. Chen H, Detmer SA, Ewald A.J., Griffin EE, Fraser SE, Chan D.C. (2003). Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J Cell Biol 160, 189-200.
6. Cipolat S, Martins de BO, Dal ZB, Scorrano L. (2004). OPA1 requires mitofusin 1 to promote mitochondrial fusion. Proc Natl Acad Sci USA 101, 15927-15932.
7. Cogliati S, Frezza C, Soriano M.E., Varanita T., Quintana-Cabrera R, Corrado M, Cipolat S., Costa V, Casarin A, Gomes L.C., et al. (2013). Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory ejficiency. Cell 155, 160-171.
8. Collins TJ, Berridge MJ, Lipp P, Bootman M.D. (2002). Mitochondria are morphologically and functionally heterogeneous within cells. EMBO J 21, 1616-1627.
9. Ehses S, Raschke I, Mancuso G., Bernacchia A, Geimer S, Tondera D., Martinou JC, Westermann B, Rugarli EI, Langer T. (2009). Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1. J Cell Biol 187, 1023-1036.
10. Frezza C, Cipolat S, Martins de BO, Micaroni M, Beznoussenko GV, Rudka T, Bartoli D., Polishuck RS, Danial NN, De S.B. (2006). OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 126, 177-189.
11. Gegg ME, Cooper JM, Chau K.Y., Rojo M., Schapira AH, Taanman J.W. (2010). Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependentmanner upon induction of mitophagy. Hum Mol Genet 19, 4861-4870.
12. Gomes LC, Di BG, Scorrano L. (2011). During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat Cell Biol 13, 589-598.
13. Guillery O, Malka F, Landes T., Guillou E, Blackstone C, Lombes A., Belenguer P, Arnoult D, Rojo M. (2008). Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential. Biol Cell 100, 315-325.
14. Hageman J, van Waarde MA, Zylicz A, Walerych D, Kampinga H.H. (2011). The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. Biochem J 435, 127-142.
15. Hartl FU, Bracher A, Hayer-Hartl M (2011). Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332.
16. Head B, Griparic L, Amiri M., Gandre-Babbe S, van der Bliek AM (2009). Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells. J Cell Biol 187, 959-966.
17. Iosefson O, Sharon S, Goloubinoff P., Azem A. (2012). Reactivation of protein aggregates by mortalin and Tid1 - the human mitochondrial Hsp70 chaperone system. Cell Stress Chaperones 17, 57-66.
18. Jendrach M, Mai S, Pohl S., Voth M, Bereiter-Hahn J (2008). Short- and longterm alterations of mitochondrial morphology, dynamics and mtDNA after transient oxidative stress. Mitochondrion 8, 293-304.
19. Kampinga HH, Craig E.A. (2010). The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 11, 579-592.
20. Kim SW, Chao TH, Xiang R, Lo J.F., Campbell MJ, Fearns C, Lee J.D. (2004). Tid1, the human homologue of a Drosophila tumor suppressor, reduces the malignant activity of ErbB-2 in carcinoma cells. Cancer Res 64, 7732-7739.
21. Lee B, Elwi AN, Meijnderta H.C., Braun JEA, Kim S-W (2012). Mitochondrial chaperone DnaJA3 induces Drp1-dependent mitochondrial fragmentation. Int J Biochem Mol Biol 44, 1366-1376.
22. Legros F, Lombes A, Frachon P., Rojo M. (2002). Mitochondrial fusion in human cells is ejficient, requires the inner membrane potential, and is mediated by mitofusins. Mol Biol Cell 13, 4343-4354.
23. Loson OC, Song Z, Chen H., Chan D.C. (2013). Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission. Mol Biol Cell 24, 659-667.
24. Norton M, Ng ACH, Baird S, Dumoulin A., Shutt T, Mah N, Andrade-Navarro MA, McBride H.M., Screaton R.B. (2014). ROMO1 is an essential redoxdependent regulator of mitochondrial dynamics. Sci Signal 7, ra10.
25. Otera H, Wang C, Cleland M.M., Setoguchi K., Yokota S, Youle RJ, Mihara K. (2010). Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J Cell Biol 191, 1141-1158.
26. Pellegrino MW, Nargund AM, Kirienko N.V., Gillis R., Fiorese CJ, Haynes C.M. (2014). Mitochondrial UPR-regulated innate immunity provides resistance to pathogen infection. Nature 516, 414-417.
27. Schmidt O, Pfanner N, Meisinger C (2010). Mitochondrial protein import: from proteomics to functional mechanisms. Nat Rev Mol Cell Biol 11, 655-667.
28. Song Z, Chen H, Fiket M., Alexander C, Chan D.C. (2007). OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J Cell Biol 178, 749-755.
29. Suen DF, Norris KL, Youle RJ (2008). Mitochondrial dynamics and apoptosis. Genes Dev 22, 1577-1590.
30. Yoon Y, Krueger EW, Oswald B.J., McNiven M.A. (2003). The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol Cell Biol 23, 5409-5420.
31. Zhao J, Liu T, Jin S., Wang X, Qu M, Uhlen P., Tomilin N, Shupliakov O, Lendahl U., Nister M. (2011). Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission. EMBO J 30, 2762-2778.