Ovarian carcinoma immunoreactive antigen-like protein 2 (OCIAD2) is a novel complex III specific assembly factor in mitochondria

2022 | journal article; research paper. A publication with affiliation to the University of Göttingen.

Jump to:Cite & Linked | Documents & Media | Details | Version history

Cite this publication

​Ovarian carcinoma immunoreactive antigen-like protein 2 (OCIAD2) is a novel complex III specific assembly factor in mitochondria​
Chojnacka, K. J.; Elancheliyan, P.; Mussulini, B. H. M.; Mohanraj, K.; Callegari, S.; Gosk, A. & Banach, T. et al.​ (2022) 
Molecular Biology of the Cell,.​ DOI: https://doi.org/10.1091/mbc.E21-03-0143 

Documents & Media

License

GRO License GRO License

Details

Authors
Chojnacka, Katarzyna Justyna; Elancheliyan, Praveenraj; Mussulini, Ben Hur Marins; Mohanraj, Karthik; Callegari, Sylvie; Gosk, Aleksandra; Banach, Tomasz; Góral, Tomasz; Szczepanowska, Karolina; Rehling, Peter 
Abstract
Assembly of the dimeric complex III (CIII 2 ) in the mitochondrial inner membrane is an intricate process, in which several accessory proteins are involved as assembly factors. Despite numerous studies, this process is yet to be fully understood. Here we report the identification of human OCIAD2 (Ovarian Carcinoma Immunoreactive Antigen domain containing protein 2) protein as an assembly factor for CIII 2 . OCIAD2 was found deregulated in several carcinomas and also in some neurogenerative disorders, however its non-pathological role had not been elucidated.  We have shown that OCIAD2 localizes to mitochondria and interacts with electron transport chain (ETC) proteins. Complete loss of OCIAD2 using gene editing in HEK293 cells resulted in abnormal mitochondrial morphology, a substantial decrease of both CIII 2 and supercomplex III 2 +IV, and reduction in CIII enzymatic activity. Identification of OCIAD2 as a protein required for assembly of functional CIII 2 provides a new insight into the biogenesis and architecture of the ETC. Elucidating the mechanism of OCIAD2 action is important both for the understanding of cellular metabolism and for an understanding of its role in malignant transformation.
Assembly of the dimeric complex III (CIII 2 ) in the mitochondrial inner membrane is an intricate process, in which several accessory proteins are involved as assembly factors. Despite numerous studies, this process is yet to be fully understood. Here we report the identification of human OCIAD2 (Ovarian Carcinoma Immunoreactive Antigen domain containing protein 2) protein as an assembly factor for CIII 2 . OCIAD2 was found deregulated in several carcinomas and also in some neurogenerative disorders, however its non-pathological role had not been elucidated.  We have shown that OCIAD2 localizes to mitochondria and interacts with electron transport chain (ETC) proteins. Complete loss of OCIAD2 using gene editing in HEK293 cells resulted in abnormal mitochondrial morphology, a substantial decrease of both CIII 2 and supercomplex III 2 +IV, and reduction in CIII enzymatic activity. Identification of OCIAD2 as a protein required for assembly of functional CIII 2 provides a new insight into the biogenesis and architecture of the ETC. Elucidating the mechanism of OCIAD2 action is important both for the understanding of cellular metabolism and for an understanding of its role in malignant transformation.
Issue Date
2022
Journal
Molecular Biology of the Cell 
Project
EXC 2067: Multiscale Bioimaging 
SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente 
SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg 
FOR 2848: Architektur und Heterogenität der inneren mitochondrialen Membran auf der Nanoskala 
FOR 2848 | P04: Analyse der räumlichen Organisation der OXPHOS Assemblierung in Säugerzellen 
Working Group
RG Rehling (Mitochondrial Protein Biogenesis) 
External URL
https://mbexc.uni-goettingen.de/literature/publications/396
https://sfb1190.med.uni-goettingen.de/production/literature/publications/169
https://for2848.gwdguser.de/literature/publications/6
ISSN
1059-1524
eISSN
1939-4586
Language
English

Reference

Citations


Social Media