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Review
. 2009 Dec;10(12):1301-5.
doi: 10.1038/embor.2009.247. Epub 2009 Nov 13.

Shaping the mitochondrion: mitochondrial biogenesis, dynamics and dysfunction. Conference on Mitochondrial Assembly and Dynamics in Health and Disease

Janet M Shaw  1 , Dennis R Winge
Affiliations
Review

Shaping the mitochondrion: mitochondrial biogenesis, dynamics and dysfunction. Conference on Mitochondrial Assembly and Dynamics in Health and Disease

Janet M Shaw et al. EMBO Rep. 2009 Dec.
No abstract available

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Conflict of interest statement

The authors declare that they have no conflict of interest.

Figures

Figure 1
Figure 1
The OXPHOS respiratory supercomplex. The OXPHOS respiratory chain is organized in supercomplexes, one of which consists of complex I, dimeric complex III and complex IV. The arrangement of the complexes in the superstructure is depicted based on the known cryoEM images of the supercomplex (Schafer et al, 2006, 2007). The cofactors in each complex are shown. Although the only structure of mammalian complex I is a cryoEM image, a crystal structure of the peripheral arm of the Thermus thermophilus complex I is available (Sazanov & Hinchliffe, 2006). In the T. hermophilus enzyme, nine distinct Fe/S centres exist, whereas the mammalian enzyme seems to have only eight Fe/S centres. The dimeric complex III contains two haem b centres in the mitochondrially encoded CytB subunit, cytochrome c1 and the Rieske 2Fe/2S centre per subunit. Complex IV contains two haem a moieties and three copper ions as redox cofactors. Electrons are passed from complex I to complex III through coenzyme Q, and from complex III to complex IV through cytochrome c. bc1, cytochrome c reductase; CcO, cytochrome c oxidase; CoQ, coenzyme Q; CryoEM, cryoelectron microscopy; Cyc, cytochrome c; Fe/S, iron/sulphur; OXPHOS, oxidative phosphorylation.
Figure 2
Figure 2
Cofactors involved in electron flux from complex II. The oxidation of succinate in the Krebs cycle by succinate dehydrogenase results in electron flux to coenzyme Q (CoQ) and subsequently to complex III, as depicted. Succinate dehydrogenase consists of four subunits with a covalently bound flavin in SDH1, three Fe/S centres in SDH2 and a haem b moiety bound between the two membrane subunits, SDH3 and SDH4 (Sun et al, 2005). bc1, cytochrome c reductase; CcO, cytochrome c oxidase; Cyc, cytochrome c; Fe/S, iron/sulphur; SDH, succinate dehydrogenase.
Figure 3
Figure 3
Mitochondria–ER attachment and function. Tethering proteins generate contact sites that hold the ER membrane and mitochondrial outer membrane (MOM) in close proximity. These contact sites also contain proteins that mediate calcium transport/signalling and lipid metabolism. ER, endoplasmic reticulum; MIM, mitochondrial inner membrane; PtdSer, phosphatidylserine; PtEtn, phosphatidylethanolamine; Ser, serine.
None
The summer research conference on Mitochondrial Assembly and Dynamics in Health and Disease took place between 5 and 10 July 2009, in Carefree, Arizona, USA, and was organized by C. Koehler and T. Langer.
None
Janet M. Shaw
None
Dennis R. Winge
See this image and copyright information in PMC

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