Assembly of the oxidative phosphorylation (OXPHOS) system in the mitochondrial inner membrane is an intricate process in which many factors must interact. The OXPHOS system is composed of four respiratory chain complexes, which are responsible for electron transport and generation of the proton gradient in the mitochondrial intermembrane space, and of the ATP synthase that uses this proton gradient to produce ATP. Mitochondrial human disorders are caused by dysfunction of the OXPHOS system, and many of them are associated with altered assembly of one or more components of the OXPHOS system. The study of assembly defects in patients has been useful in unraveling and/or gaining a complete understanding of the processes by which these large multimeric complexes are formed. We review here current knowledge of the biogenesis of OXPHOS complexes based on investigation of the corresponding disorders.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.bbamcr.2008.05.028 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Selection of initiator tRNA and start codon by mammalian mitochondrial initiation factor 3 in leaderless mRNA translation.
Nucleic Acids Res
January 2025
Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5, Kashiwanoha, Kashiwa-shi, Chiba 277-8562, Japan.
Article Synopsis
- The mammalian mitochondrial protein synthesis system is responsible for synthesizing 13 crucial subunits for energy production, but the exact role of IF-3mt in translation initiation is still unclear.
- Researchers created a mitochondrial translation system to explore IF-3mt's proofreading abilities, revealing it helps distinguish between different start codons for more accurate protein synthesis.
- The findings indicate that IF-3mt not only supports initiation from standard AUG start codons but can also facilitate initiation from non-AUG codons like AUA, highlighting its adaptability in working with leaderless mRNAs.
Mitochondrial retrograde signaling (MRS) pathways relay the functional status of mitochondria to elicit homeostatic or adaptive changes in nuclear gene expression. Budding yeast have "intergenomic signaling" pathways that sense the amount of mitochondrial DNA (mtDNA) independently of oxidative phosphorylation (OXPHOS), the primary function of genes encoded by mtDNA. However, MRS pathways that sense the amount of mtDNA in mammalian cells remain poorly understood.
View Article and Find Full Text PDFLong-Term Effects of Radiation Therapy on Cerebral Microvessel Proteome: A Six-Month Post-Exposure Analysis.
bioRxiv
January 2025
Abboud Cardiovascular Research Center, Department of Internal Medicine, Carver College of Medicine, University of Iowa.
Background: Radiation therapy (RT) treats primary and metastatic brain tumors, with about one million Americans surviving beyond six months post-treatment. However, up to 90% of survivors experience RT-induced cognitive impairment. Emerging evidence links cognitive decline to RT-induced endothelial dysfunction in brain microvessels, yet studies of endothelial injury remain limited.
View Article and Find Full Text PDFEpigenetic Threads of Neurodegeneration: TFAM's Intricate Role in Mitochondrial Transcription.
CNS Neurol Disord Drug Targets
January 2025
Department of Pharmaceutical Chemistry, JSS College of Pharmacy, Mysuru 570015. JSS Academy of Higher Education and Research, Mysuru, Karnataka, India.
There is a myriad of activities that involve mitochondria that are crucial for maintaining cellular equilibrium and genetic stability. In the pathophysiology of neurodegenerative illnesses, mitochondrial transcription influences mitochondrial equilibrium, which in turn affects their biogenesis and integrity. Among the crucial proteins for keeping the genome in optimal repair is mitochondrial transcription factor A, more commonly termed TFAM.
View Article and Find Full Text PDFGlobal cellular proteo-lipidomic profiling of diverse lysosomal storage disease mutants using nMOST.
Sci Adv
January 2025
Department of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.
Lysosomal storage diseases (LSDs) comprise ~50 monogenic disorders marked by the buildup of cellular material in lysosomes, yet systematic global molecular phenotyping of proteins and lipids is lacking. We present a nanoflow-based multiomic single-shot technology (nMOST) workflow that quantifies HeLa cell proteomes and lipidomes from over two dozen LSD mutants. Global cross-correlation analysis between lipids and proteins identified autophagy defects, notably the accumulation of ferritinophagy substrates and receptors, especially in and mutants, where lysosomes accumulate cholesterol.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!