New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of <i>Oryctolagus cuniculus</i>
To date, some scientific evidence (limited proteolysis, mass spectrometry analysis, electron microscopy (EM)) has accumulated, which indicates that the generally accepted model of double-stranded of filamentous actin (F-actin) organization in eukaryotic cells is not the only one. This entails an amb...
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| Format: | Article |
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MDPI AG
2020-11-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/21/8319 |
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| author | Anna V. Glyakina Alexey K. Surin Sergei Yu. Grishin Olga M. Selivanova Mariya Yu. Suvorina Liya G. Bobyleva Ivan M. Vikhlyantsev Oxana V. Galzitskaya |
| author_facet | Anna V. Glyakina Alexey K. Surin Sergei Yu. Grishin Olga M. Selivanova Mariya Yu. Suvorina Liya G. Bobyleva Ivan M. Vikhlyantsev Oxana V. Galzitskaya |
| author_sort | Anna V. Glyakina |
| collection | DOAJ |
| description | To date, some scientific evidence (limited proteolysis, mass spectrometry analysis, electron microscopy (EM)) has accumulated, which indicates that the generally accepted model of double-stranded of filamentous actin (F-actin) organization in eukaryotic cells is not the only one. This entails an ambiguous understanding of many of the key cellular processes in which F-actin is involved. For a detailed understanding of the mechanism of F-actin assembly and actin interaction with its partners, it is necessary to take into account the polymorphism of the structural organization of F-actin at the molecular level. Using electron microscopy, limited proteolysis, mass spectrometry, X-ray diffraction, and structural modeling we demonstrated that F-actin presented in the EM images has no double-stranded organization, the regions of protease resistance are accessible for action of proteases in F-actin models. Based on all data, a new spatial model of filamentous actin is proposed, and the F-actin polymorphism is discussed. |
| first_indexed | 2024-03-10T15:02:54Z |
| format | Article |
| id | doaj.art-3a7c6a6147724311a36bd445a65d5b59 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T15:02:54Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-3a7c6a6147724311a36bd445a65d5b592023-11-20T19:58:11ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-012121831910.3390/ijms21218319New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of <i>Oryctolagus cuniculus</i>Anna V. Glyakina0Alexey K. Surin1Sergei Yu. Grishin2Olga M. Selivanova3Mariya Yu. Suvorina4Liya G. Bobyleva5Ivan M. Vikhlyantsev6Oxana V. Galzitskaya7Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaTo date, some scientific evidence (limited proteolysis, mass spectrometry analysis, electron microscopy (EM)) has accumulated, which indicates that the generally accepted model of double-stranded of filamentous actin (F-actin) organization in eukaryotic cells is not the only one. This entails an ambiguous understanding of many of the key cellular processes in which F-actin is involved. For a detailed understanding of the mechanism of F-actin assembly and actin interaction with its partners, it is necessary to take into account the polymorphism of the structural organization of F-actin at the molecular level. Using electron microscopy, limited proteolysis, mass spectrometry, X-ray diffraction, and structural modeling we demonstrated that F-actin presented in the EM images has no double-stranded organization, the regions of protease resistance are accessible for action of proteases in F-actin models. Based on all data, a new spatial model of filamentous actin is proposed, and the F-actin polymorphism is discussed.https://www.mdpi.com/1422-0067/21/21/8319actinmonomerfilamentproteolysisaccessible surface areamass spectrometry |
| spellingShingle | Anna V. Glyakina Alexey K. Surin Sergei Yu. Grishin Olga M. Selivanova Mariya Yu. Suvorina Liya G. Bobyleva Ivan M. Vikhlyantsev Oxana V. Galzitskaya New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of <i>Oryctolagus cuniculus</i> International Journal of Molecular Sciences actin monomer filament proteolysis accessible surface area mass spectrometry |
| title | New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of <i>Oryctolagus cuniculus</i> |
| title_full | New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of <i>Oryctolagus cuniculus</i> |
| title_fullStr | New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of <i>Oryctolagus cuniculus</i> |
| title_full_unstemmed | New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of <i>Oryctolagus cuniculus</i> |
| title_short | New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of <i>Oryctolagus cuniculus</i> |
| title_sort | new model for stacking monomers in filamentous actin from skeletal muscles of i oryctolagus cuniculus i |
| topic | actin monomer filament proteolysis accessible surface area mass spectrometry |
| url | https://www.mdpi.com/1422-0067/21/21/8319 |
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