Desmin Interacts Directly with Mitochondria
| Autor: | Alexander A. Minin, Natalia V. Medvedeva, Alexey K. Surin, Tatiana M Nekrasova, Alexander A Dayal, Sergey D Duhalin |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
intermediate filaments
Mutant mitochondria desmin calpain macromolecular substances Mitochondrion Article Catalysis Inorganic Chemistry lcsh:Chemistry Cysteine Proteases Animals Humans Vimentin Myocyte Physical and Theoretical Chemistry Intermediate filament Molecular Biology lcsh:QH301-705.5 Cells Cultured Spectroscopy biology Chemistry Organic Chemistry Calpain General Medicine musculoskeletal system Cysteine protease Rats Computer Science Applications Cell biology lcsh:Biology (General) lcsh:QD1-999 biology.protein Desmin Myofibril |
| Zdroj: | International Journal of Molecular Sciences, Vol 21, Iss 8122, p 8122 (2020) International Journal of Molecular Sciences; Volume 21; Issue 21; Pages: 8122 International Journal of Molecular Sciences |
| ISSN: | 1661-6596 1422-0067 |
| Popis: | Desmin intermediate filaments (IFs) play an important role in maintaining the structural and functional integrity of muscle cells. They connect contractile myofibrils to plasma membrane, nuclei, and mitochondria. Disturbance of their network due to desmin mutations or deficiency leads to an infringement of myofibril organization and to a deterioration of mitochondrial distribution, morphology, and functions. The nature of the interaction of desmin IFs with mitochondria is not clear. To elucidate the possibility that desmin can directly bind to mitochondria, we have undertaken the study of their interaction in vitro. Using desmin mutant Des(Y122L) that forms unit-length filaments (ULFs) but is incapable of forming long filaments and, therefore, could be effectively separated from mitochondria by centrifugation through sucrose gradient, we probed the interaction of recombinant human desmin with mitochondria isolated from rat liver. Our data show that desmin can directly bind to mitochondria, and this binding depends on its N-terminal domain. We have found that mitochondrial cysteine protease can disrupt this interaction by cleavage of desmin at its N-terminus. |
| Databáze: | OpenAIRE |
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