Benischke, Anne-Sophie. Ubiquitin-proteasome dependent mitochondrial protein quality control. 2014, PhD Thesis, University of Basel, Faculty of Science.
Official URL: http://edoc.unibas.ch/diss/DissB_10774
Not only reactive oxygen species are involved in the aging process and in neurodegeneration, other stressors such as reactive nitrogen species, especially nitric oxide (NO) also cause such damage. Constant low level damage caused by NO to mitochondria eventually results in the loss of mitochondrial integrity and ultimately mitochondrial dysfunction. NO can directly modify mitochondrial proteins in a reaction, called S-nitrosylation. In response to low level of exogenous NO but also in the absence of such exogenous nitrosative stress, S-nitrosylated proteins are present in mitochondria. Furthermore, we found that upon inhibition of the proteasome, levels of S-nitrosylated proteins are increased and that the AAA-ATPase p97 is involved in the translocation of such S-nitrosylated proteins from mitochondria into the cytosol.
Taken together, OMMAD components are necessary for maintaining mitochondrial integrity on the molecular and on the organellar level through the removal of damaged proteins and through regulating mitochondrial morphology.
|Committee Members:||Neutzner, Albert and Huwyler, Jörg|
|Faculties and Departments:||03 Faculty of Medicine > Departement Biomedizin > Associated Research Groups > Pharmakologie (Handschin)|
|Bibsysno:||Link to catalogue|
|Number of Pages:||98 Bl.|
|Last Modified:||30 Jun 2016 10:55|
|Deposited On:||21 May 2014 15:25|
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