Quality Control of Mitochondrial Proteostasis

Overview

Journal Cold Spring Harb Perspect Biol

Specialties Biology
Molecular Biology

Date 2011 Jun 2

PMID 21628427

Citations 140

Authors

Michael J Baker

Takashi Tatsuta

Thomas Langer

Affiliations

Soon will be listed here.

Abstract

A decline in mitochondrial activity has been associated with aging and is a hallmark of many neurological diseases. Surveillance mechanisms acting at the molecular, organellar, and cellular level monitor mitochondrial integrity and ensure the maintenance of mitochondrial proteostasis. Here we will review the central role of mitochondrial chaperones and proteases, the cytosolic ubiquitin-proteasome system, and the mitochondrial unfolded response in this interconnected quality control network, highlighting the dual function of some proteases in protein quality control within the organelle and for the regulation of mitochondrial fusion and mitophagy.

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References

Delettre C, Griffoin J, Kaplan J, Dollfus H, Lorenz B, Faivre L . Mutation spectrum and splicing variants in the OPA1 gene. Hum Genet. 2002; 109(6):584-91. DOI: 10.1007/s00439-001-0633-y. View

Suzuki Y, Takahashi-Niki K, Akagi T, Hashikawa T, Takahashi R . Mitochondrial protease Omi/HtrA2 enhances caspase activation through multiple pathways. Cell Death Differ. 2003; 11(2):208-16. DOI: 10.1038/sj.cdd.4401343. View

Osman C, Wilmes C, Tatsuta T, Langer T . Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase. Mol Biol Cell. 2006; 18(2):627-35. PMC: 1783772. DOI: 10.1091/mbc.e06-09-0839. View

Chen H, Chomyn A, Chan D . Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem. 2005; 280(28):26185-92. DOI: 10.1074/jbc.M503062200. View

Hohfeld J, Hartl F . Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. J Cell Biol. 1994; 126(2):305-15. PMC: 2200036. DOI: 10.1083/jcb.126.2.305. View

Zeng X, Neupert W, Tzagoloff A . The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase. Mol Biol Cell. 2006; 18(2):617-26. PMC: 1783785. DOI: 10.1091/mbc.e06-09-0801. View

Dunn C, Tamura Y, Sesaki H, Jensen R . Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex. Mol Biol Cell. 2008; 19(12):5387-97. PMC: 2592643. DOI: 10.1091/mbc.e08-01-0103. View

Moisoi N, Klupsch K, Fedele V, East P, Sharma S, Renton A . Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response. Cell Death Differ. 2008; 16(3):449-64. DOI: 10.1038/cdd.2008.166. View

Rodolfo C, Ciccosanti F, Di Giacomo G, Piacentini M, Fimia G . Proteomic analysis of mitochondrial dysfunction in neurodegenerative diseases. Expert Rev Proteomics. 2010; 7(4):519-42. DOI: 10.1586/epr.10.43. View

10.

Satoh M, Hamamoto T, Seo N, Kagawa Y, Endo H . Differential sublocalization of the dynamin-related protein OPA1 isoforms in mitochondria. Biochem Biophys Res Commun. 2002; 300(2):482-93. DOI: 10.1016/s0006-291x(02)02874-7. View

11.

Pinton P, Brini M, Bastianutto C, Tuft R, Pozzan T, Rizzuto R . New light on mitochondrial calcium. Biofactors. 1999; 8(3-4):243-53. DOI: 10.1002/biof.5520080312. View

12.

Hansen J, Gregersen N, Bross P . Differential degradation of variant medium-chain acyl-CoA dehydrogenase by the protein quality control proteases Lon and ClpXP. Biochem Biophys Res Commun. 2005; 333(4):1160-70. DOI: 10.1016/j.bbrc.2005.06.024. View

13.

Koppen M, Langer T . Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases. Crit Rev Biochem Mol Biol. 2007; 42(3):221-42. DOI: 10.1080/10409230701380452. View

14.

Youle R, Narendra D . Mechanisms of mitophagy. Nat Rev Mol Cell Biol. 2010; 12(1):9-14. PMC: 4780047. DOI: 10.1038/nrm3028. View

15.

Kim K, Park S, Kang S, Cheong G, Chung C . Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli. J Mol Biol. 1999; 294(5):1363-74. DOI: 10.1006/jmbi.1999.3320. View

16.

Griparic L, Kanazawa T, van der Bliek A . Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage. J Cell Biol. 2007; 178(5):757-64. PMC: 2064541. DOI: 10.1083/jcb.200704112. View

17.

Livnat-Levanon N, Glickman M . Ubiquitin-proteasome system and mitochondria - reciprocity. Biochim Biophys Acta. 2010; 1809(2):80-7. DOI: 10.1016/j.bbagrm.2010.07.005. View

18.

Escobar-Henriques M, Westermann B, Langer T . Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1. J Cell Biol. 2006; 173(5):645-50. PMC: 2063881. DOI: 10.1083/jcb.200512079. View

19.

Song Z, Chen H, Fiket M, Alexander C, Chan D . OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J Cell Biol. 2007; 178(5):749-55. PMC: 2064540. DOI: 10.1083/jcb.200704110. View

20.

Jin S, Lazarou M, Wang C, Kane L, Narendra D, Youle R . Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Biol. 2010; 191(5):933-42. PMC: 2995166. DOI: 10.1083/jcb.201008084. View