Dennerlein 2014 Abstract IOC96
Dennerlein S (2014) Insights into COX-assembly: An important but not the only OXPHOS complex. Mitochondr Physiol Network 19.11. |
Link:
Dennerlein S, Oeljeklaus S, Warscheid B, Rehling P (2014)
Event: IOC96
Within the last decades the development of a broad range of diagnostic methodologies led to the identification of an increasing number of human mitochondrial disease genes. Many patients present defects in the mitochondrial oxidative phosphorylation system (OXPHOS), the main energy source of the cell. The OXPHOS system is composed of the ATP producing ATP synthase (complex V), and of four multisubunit enzyme complexes, the mitochondrial respiratory chain (MRC) or complexes I-IV. In addition to the 82 structural components, an increasing number of associated factors, required for complex assembly, have been described. In contrast to the nuclear-encoded structural components, mutations in several COX assembly factors have been reported and were shown to be associated with various disorders. However, beside the growing number of identified MRC assembly factors, the understanding of the molecular mechanisms of complex IV assembly and maturation is far from complete.
We have recently identified a novel player, MITRAC12, which was shown to be in association with SURF1, a COX assembly factor, mutated in Leigh syndrome. This finding led to the identification of the MITRAC complex, a COX assembly intermediate. We have shown that MITRAC components feed back to COX1 translation and further facilitate the integration of newly imported nuclear encoded COX-subunits in the maturing enzyme via TIM21. However, the data support also an involvement of TIM21 in the maturation of all other OXPHOS complexes. Hence it is essential to get quantitative data of the activity and functionality of these complexes.
β’ O2k-Network Lab: DE Goettingen Dennerlein S
Labels: MiParea: Respiration, Patients
Stress:Mitochondrial disease Organism: Human
Coupling state: OXPHOS
MITRAC12
Affiliation
Inst Cellular Biochemistry, Univ GΓΆttingen, Germany
Inst Biology, Fac Biology, Functional Proteomics, Univ Freiburg
BIOSS Centre Biol Signalling Studies
Max Planck Inst Biophysical Chemistry, GΓΆttingen
Germany