A AAA ATPase Cdc48 with a cofactor Ubx2 facilitates ubiquitylation of a mitochondrial fusion-promoting factor Fzo1 for proteasomal degradation
| Autor: | Abhijit Chowdhury, Teru Ogura, Masatoshi Esaki, Sabiqun Nahar |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Proteasome Endopeptidase Complex
Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Mitochondrion Mitochondrial Dynamics Biochemistry Cofactor GTP Phosphohydrolases Mitochondrial Proteins 03 medical and health sciences 0302 clinical medicine Ubiquitin Valosin Containing Protein Endopeptidases Translocase Molecular Biology 030304 developmental biology Adenosine Triphosphatases 0303 health sciences biology Catabolism Chemistry Ubiquitination Membrane Proteins General Medicine AAA proteins Mitochondria Cell biology mitochondrial fusion Mitochondrial Membranes biology.protein Carrier Proteins Bacterial outer membrane 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | The Journal of Biochemistry. 167:279-286 |
| ISSN: | 1756-2651 0021-924X |
| Popis: | Dynamic functionality of mitochondria is maintained by continual fusion and fission events. A mitochondrial outer membrane protein Fzo1 plays a pivotal role upon mitochondrial fusion by homo-oligomerization to tether fusing mitochondria. Fzo1 is tightly regulated by ubiquitylations and the ubiquitin-responsible AAA protein Cdc48. Here, we show that a Cdc48 cofactor Ubx2 facilitates Fzo1 turnover. The Cdc48-Ubx2 complex has been shown to facilitate degradation of ubiquitylated proteins stacked at the protein translocation complex in the mitochondrial outer membrane by releasing them from the translocase. By contrast, in the degradation process of Fzo1, the Cdc48-Ubx2 complex appears to facilitate the degradation-signalling ubiquitylation of the substrate itself. In addition, the Cdc48-Ubx2 complex interacts with Ubp2, a deubiquitylase reversing the degradation-signalling ubiquitylation of Fzo1. These results suggest that the Cdc48-Ubx2 complex regulates Fzo1 turnover by modulating ubiquitylation status of the substrate. |
| Databáze: | OpenAIRE |
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