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Crit Rev Biochem Mol Biol. 2015 Mar-Apr;50(2):168-80. doi: 10.3109/10409238.2014.990556. Epub 2014 Dec 9.

Protein-mediated assembly of succinate dehydrogenase and its cofactors.

Author information

1
Department of Biochemistry and.

Abstract

Succinate dehydrogenase (or complex II; SDH) is a heterotetrameric protein complex that links the tribarboxylic acid cycle with the electron transport chain. SDH is composed of four nuclear-encoded subunits that must translocate independently to the mitochondria and assemble into a mature protein complex embedded in the inner mitochondrial membrane. Recently, it has become clear that failure to assemble functional SDH complexes can result in cancer and neurodegenerative syndromes. The effort to thoroughly elucidate the SDH assembly pathway has resulted in the discovery of four subunit-specific assembly factors that aid in the maturation of individual subunits and support the assembly of the intact complex. This review will focus on these assembly factors and assess the contribution of each factor to the assembly of SDH. Finally, we propose a model of the SDH assembly pathway that incorporates all extant data.

KEYWORDS:

Assembly factors; redox-active cofactors; respiratory chain; succinate dehydrogenase

PMID:
25488574
PMCID:
PMC4653115
DOI:
10.3109/10409238.2014.990556
[Indexed for MEDLINE]
Free PMC Article

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