Desmin Interacts Directly with Mitochondria
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 infringe...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-10-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/21/8122 |
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| author | Alexander A. Dayal Natalia V. Medvedeva Tatiana M. Nekrasova Sergey D. Duhalin Alexey K. Surin Alexander A. Minin |
| author_facet | Alexander A. Dayal Natalia V. Medvedeva Tatiana M. Nekrasova Sergey D. Duhalin Alexey K. Surin Alexander A. Minin |
| author_sort | Alexander A. Dayal |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T15:12:41Z |
| format | Article |
| id | doaj.art-23a5c011750840f7b29a9b0f86568ed8 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T15:12:41Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-23a5c011750840f7b29a9b0f86568ed82023-11-20T19:13:10ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-10-012121812210.3390/ijms21218122Desmin Interacts Directly with MitochondriaAlexander A. Dayal0Natalia V. Medvedeva1Tatiana M. Nekrasova2Sergey D. Duhalin3Alexey K. Surin4Alexander A. Minin5Institute of Protein Research of Russian Academy of Sciences, Vavilova st., 34, 119334 Moscow, RussiaInstitute of Protein Research of Russian Academy of Sciences, Vavilova st., 34, 119334 Moscow, RussiaInstitute of Protein Research of Russian Academy of Sciences, Vavilova st., 34, 119334 Moscow, RussiaInstitute of Protein Research of Russian Academy of Sciences, Vavilova st., 34, 119334 Moscow, RussiaInstitute of Protein Research of Russian Academy of Sciences, Vavilova st., 34, 119334 Moscow, RussiaInstitute of Protein Research of Russian Academy of Sciences, Vavilova st., 34, 119334 Moscow, RussiaDesmin 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.https://www.mdpi.com/1422-0067/21/21/8122mitochondriadesminintermediate filamentscalpain |
| spellingShingle | Alexander A. Dayal Natalia V. Medvedeva Tatiana M. Nekrasova Sergey D. Duhalin Alexey K. Surin Alexander A. Minin Desmin Interacts Directly with Mitochondria International Journal of Molecular Sciences mitochondria desmin intermediate filaments calpain |
| title | Desmin Interacts Directly with Mitochondria |
| title_full | Desmin Interacts Directly with Mitochondria |
| title_fullStr | Desmin Interacts Directly with Mitochondria |
| title_full_unstemmed | Desmin Interacts Directly with Mitochondria |
| title_short | Desmin Interacts Directly with Mitochondria |
| title_sort | desmin interacts directly with mitochondria |
| topic | mitochondria desmin intermediate filaments calpain |
| url | https://www.mdpi.com/1422-0067/21/21/8122 |
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