دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: Ovarian carcinoma immunoreactive antigen-like protein 2 (OCIAD2) is a novel complex III-specific assembly factor in mitochondria.
المؤلفون: Chojnacka KJ; Centre of New Technologies, University of Warsaw, 02-097 Warsaw, Poland., Elancheliyan P; ReMedy International Research Agenda Unit, International Institute of Molecular Mechanisms and Machines (IMol), Polish Academy of Sciences, 00-783 Warsaw, Poland., Mussulini BHM; ReMedy International Research Agenda Unit, International Institute of Molecular Mechanisms and Machines (IMol), Polish Academy of Sciences, 00-783 Warsaw, Poland., Mohanraj K; ReMedy International Research Agenda Unit, International Institute of Molecular Mechanisms and Machines (IMol), Polish Academy of Sciences, 00-783 Warsaw, Poland., Callegari S; Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research, Parkville 3052, Victoria, Australia.; Department of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany., Gosk A; Centre of New Technologies, University of Warsaw, 02-097 Warsaw, Poland., Banach T; ReMedy International Research Agenda Unit, International Institute of Molecular Mechanisms and Machines (IMol), Polish Academy of Sciences, 00-783 Warsaw, Poland., Góral T; Centre of New Technologies, University of Warsaw, 02-097 Warsaw, Poland., Szczepanowska K; ReMedy International Research Agenda Unit, International Institute of Molecular Mechanisms and Machines (IMol), Polish Academy of Sciences, 00-783 Warsaw, Poland., Rehling P; Department of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.; Cluster of Excellence 'Multiscale Bioimaging: from Molecular Machines to Networks of Excitable Cells' (MBExC), University of Goettingen, 37075 Göttingen, Germany.; Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany., Serwa RA; ReMedy International Research Agenda Unit, International Institute of Molecular Mechanisms and Machines (IMol), Polish Academy of Sciences, 00-783 Warsaw, Poland., Chacinska A; ReMedy International Research Agenda Unit, International Institute of Molecular Mechanisms and Machines (IMol), Polish Academy of Sciences, 00-783 Warsaw, Poland.
المصدر: Molecular biology of the cell [Mol Biol Cell] 2022 Apr 01; Vol. 33 (4), pp. ar29. Date of Electronic Publication: 2022 Jan 26.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Society for Cell Biology Country of Publication: United States NLM ID: 9201390 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1939-4586 (Electronic) Linking ISSN: 10591524 NLM ISO Abbreviation: Mol Biol Cell Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Bethesda, MD : American Society for Cell Biology, c1992-
مواضيع طبية MeSH: Carcinoma*/metabolism , Ovarian Neoplasms*/metabolism, Electron Transport Complex III/metabolism ; Female ; HEK293 Cells ; Humans ; Mitochondria/metabolism ; Neoplasm Proteins/metabolism
مستخلص: 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 has yet to be fully understood. Here we report the identification of human OCIAD2 (ovarian carcinoma immunoreactive antigen-like protein 2) as an assembly factor for CIII 2 . OCIAD2 was found to be deregulated in several carcinomas and also in some neurogenerative disorders; however, its nonpathological 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 a 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 .
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المشرفين على المادة: 0 (Neoplasm Proteins)
0 (OCIAD2 protein, human)
EC 7.1.1.8 (Electron Transport Complex III)
تواريخ الأحداث: Date Created: 20220126 Date Completed: 20220411 Latest Revision: 20220716
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC9250361
DOI: 10.1091/mbc.E21-03-0143
PMID: 35080992
قاعدة البيانات: MEDLINE
الوصف
تدمد:1939-4586
DOI:10.1091/mbc.E21-03-0143