Dataset Information

Mutations in CYC1, encoding cytochrome c1 subunit of respiratory chain complex III, cause insulin-responsive hyperglycemia.

ABSTRACT: Many individuals with abnormalities of mitochondrial respiratory chain complex III remain genetically undefined. Here, we report mutations (c.288G>T [p.Trp96Cys] and c.643C>T [p.Leu215Phe]) in CYC1, encoding the cytochrome c1 subunit of complex III, in two unrelated children presenting with recurrent episodes of ketoacidosis and insulin-responsive hyperglycemia. Cytochrome c1, the heme-containing component of complex III, mediates the transfer of electrons from the Rieske iron-sulfur protein to cytochrome c. Cytochrome c1 is present at reduced levels in the skeletal muscle and skin fibroblasts of affected individuals. Moreover, studies on yeast mutants and affected individuals' fibroblasts have shown that exogenous expression of wild-type CYC1 rescues complex III activity, demonstrating the deleterious effect of each mutation on cytochrome c1 stability and complex III activity.

SUBMITTER: Gaignard P

PROVIDER: S-EPMC3738829 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Mutations in CYC1, encoding cytochrome c1 subunit of respiratory chain complex III, cause insulin-responsive hyperglycemia.

Gaignard Pauline P Menezes Minal M Schiff Manuel M Bayot Aurélien A Rak Malgorzata M Ogier de Baulny Hélène H Su Chen-Hsien CH Gilleron Mylene M Lombes Anne A Abida Heni H Tzagoloff Alexander A Riley Lisa L Cooper Sandra T ST Mina Kym K Sivadorai Padma P Davis Mark R MR Allcock Richard J N RJ Kresoje Nina N Laing Nigel G NG Thorburn David R DR Slama Abdelhamid A Christodoulou John J Rustin Pierre P

American journal of human genetics 20130801 2

Many individuals with abnormalities of mitochondrial respiratory chain complex III remain genetically undefined. Here, we report mutations (c.288G>T [p.Trp96Cys] and c.643C>T [p.Leu215Phe]) in CYC1, encoding the cytochrome c1 subunit of complex III, in two unrelated children presenting with recurrent episodes of ketoacidosis and insulin-responsive hyperglycemia. Cytochrome c1, the heme-containing component of complex III, mediates the transfer of electrons from the Rieske iron-sulfur protein to ...[more]

PMID: 23910460

Dataset Information

Mutations in CYC1, encoding cytochrome c1 subunit of respiratory chain complex III, cause insulin-responsive hyperglycemia.

Publications

Mutations in CYC1, encoding cytochrome c1 subunit of respiratory chain complex III, cause insulin-responsive hyperglycemia.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Similar Datasets

Recessive mutations in POLR3B, encoding the second largest subunit of Pol III, cause a rare hypomyelinating leukodystrophy.
| S-EPMC3213403 | biostudies-literature

Mutations of POLR3A encoding a catalytic subunit of RNA polymerase Pol III cause a recessive hypomyelinating leukodystrophy.
| S-EPMC3169829 | biostudies-literature

Mitochondrial cytochrome c1 is a collapsed di-heme cytochrome.
| S-EPMC539742 | biostudies-literature

Transient kinetics of subunit-III-depleted cytochrome c oxidase.
| S-EPMC1146609 | biostudies-other

Mutations in APOPT1, encoding a mitochondrial protein, cause cavitating leukoencephalopathy with cytochrome c oxidase deficiency.
| S-EPMC4157140 | biostudies-literature

Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency.
| S-EPMC4908180 | biostudies-literature

Photobiomodulation therapy ameliorates hyperglycemia and insulin resistance by activating cytochrome c oxidase-mediated protein kinase B in muscle.
| S-EPMC8064177 | biostudies-literature

Recessive mutations in KCNJ13, encoding an inwardly rectifying potassium channel subunit, cause leber congenital amaurosis.
| S-EPMC3135807 | biostudies-literature

Caspase cleavage of cytochrome c1 disrupts mitochondrial function and enhances cytochrome c release.
| S-EPMC3351920 | biostudies-literature

Mucolipidosis III GNPTG Missense Mutations Cause Misfolding of the ? Subunit of GlcNAc-1-Phosphotransferase.
| S-EPMC4907843 | biostudies-literature