Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels
Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on...
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| Autor*in: |
Kopylova, Galina V. [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Nature Switzerland AG 2019 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of muscle research and cell motility - Springer International Publishing, 1980, 40(2019), 3-4 vom: 23. Okt., Seite 299-308 |
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| Übergeordnetes Werk: |
volume:40 ; year:2019 ; number:3-4 ; day:23 ; month:10 ; pages:299-308 |
| Links: |
|---|
| DOI / URN: |
10.1007/s10974-019-09560-8 |
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| Katalog-ID: |
OLC2067131508 |
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| 520 | |a Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on the properties of single actin–myosin interactions and the characteristics of the calcium regulation in an ensemble of myosin molecules immobilised on a glass surface and interacting with regulated thin filaments. Previously, we showed that at saturating $ Ca^{2+} $ concentration the presence of Tpm on the actin filament increases the duration of the interaction. Here, we found that the studied Tpm mutations differently affected the duration: the D175N mutation reduced it compared to WT Tpm, while the E180G mutation increased it. Both dilated mutations made the duration of the interaction even shorter than with F-actin. The duration of the attached state of myosin to the thin filament in the optical trap did not correlate to the sliding velocity of thin filaments and its calcium sensitivity in the in vitro motility assay. We suppose that at the level of the molecular ensemble, the cooperative mechanisms prevail in the manifestation of the effects of cardiomyopathy-associated mutations in Tpm. | ||
| 650 | 4 | |a Actin–myosin interaction | |
| 650 | 4 | |a Tropomyosin | |
| 650 | 4 | |a Cardiomyopathy mutation | |
| 650 | 4 | |a Calcium regulation | |
| 650 | 4 | |a In vitro motility assay | |
| 650 | 4 | |a Optical trap | |
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| 700 | 1 | |a Nabiev, Salavat R. |4 aut | |
| 700 | 1 | |a Matyushenko, Alexander M. |4 aut | |
| 700 | 1 | |a Koubassova, Natalia A. |4 aut | |
| 700 | 1 | |a Levitsky, Dmitrii I. |4 aut | |
| 700 | 1 | |a Bershitsky, Sergey Y. |4 aut | |
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10.1007/s10974-019-09560-8 doi (DE-627)OLC2067131508 (DE-He213)s10974-019-09560-8-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Kopylova, Galina V. verfasserin (orcid)0000-0003-2976-2108 aut Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Nature Switzerland AG 2019 Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on the properties of single actin–myosin interactions and the characteristics of the calcium regulation in an ensemble of myosin molecules immobilised on a glass surface and interacting with regulated thin filaments. Previously, we showed that at saturating $ Ca^{2+} $ concentration the presence of Tpm on the actin filament increases the duration of the interaction. Here, we found that the studied Tpm mutations differently affected the duration: the D175N mutation reduced it compared to WT Tpm, while the E180G mutation increased it. Both dilated mutations made the duration of the interaction even shorter than with F-actin. The duration of the attached state of myosin to the thin filament in the optical trap did not correlate to the sliding velocity of thin filaments and its calcium sensitivity in the in vitro motility assay. We suppose that at the level of the molecular ensemble, the cooperative mechanisms prevail in the manifestation of the effects of cardiomyopathy-associated mutations in Tpm. Actin–myosin interaction Tropomyosin Cardiomyopathy mutation Calcium regulation In vitro motility assay Optical trap Shchepkin, Daniil V. aut Nabiev, Salavat R. aut Matyushenko, Alexander M. aut Koubassova, Natalia A. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 40(2019), 3-4 vom: 23. Okt., Seite 299-308 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:40 year:2019 number:3-4 day:23 month:10 pages:299-308 https://doi.org/10.1007/s10974-019-09560-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4219 AR 40 2019 3-4 23 10 299-308 |
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10.1007/s10974-019-09560-8 doi (DE-627)OLC2067131508 (DE-He213)s10974-019-09560-8-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Kopylova, Galina V. verfasserin (orcid)0000-0003-2976-2108 aut Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Nature Switzerland AG 2019 Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on the properties of single actin–myosin interactions and the characteristics of the calcium regulation in an ensemble of myosin molecules immobilised on a glass surface and interacting with regulated thin filaments. Previously, we showed that at saturating $ Ca^{2+} $ concentration the presence of Tpm on the actin filament increases the duration of the interaction. Here, we found that the studied Tpm mutations differently affected the duration: the D175N mutation reduced it compared to WT Tpm, while the E180G mutation increased it. Both dilated mutations made the duration of the interaction even shorter than with F-actin. The duration of the attached state of myosin to the thin filament in the optical trap did not correlate to the sliding velocity of thin filaments and its calcium sensitivity in the in vitro motility assay. We suppose that at the level of the molecular ensemble, the cooperative mechanisms prevail in the manifestation of the effects of cardiomyopathy-associated mutations in Tpm. Actin–myosin interaction Tropomyosin Cardiomyopathy mutation Calcium regulation In vitro motility assay Optical trap Shchepkin, Daniil V. aut Nabiev, Salavat R. aut Matyushenko, Alexander M. aut Koubassova, Natalia A. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 40(2019), 3-4 vom: 23. Okt., Seite 299-308 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:40 year:2019 number:3-4 day:23 month:10 pages:299-308 https://doi.org/10.1007/s10974-019-09560-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4219 AR 40 2019 3-4 23 10 299-308 |
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10.1007/s10974-019-09560-8 doi (DE-627)OLC2067131508 (DE-He213)s10974-019-09560-8-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Kopylova, Galina V. verfasserin (orcid)0000-0003-2976-2108 aut Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Nature Switzerland AG 2019 Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on the properties of single actin–myosin interactions and the characteristics of the calcium regulation in an ensemble of myosin molecules immobilised on a glass surface and interacting with regulated thin filaments. Previously, we showed that at saturating $ Ca^{2+} $ concentration the presence of Tpm on the actin filament increases the duration of the interaction. Here, we found that the studied Tpm mutations differently affected the duration: the D175N mutation reduced it compared to WT Tpm, while the E180G mutation increased it. Both dilated mutations made the duration of the interaction even shorter than with F-actin. The duration of the attached state of myosin to the thin filament in the optical trap did not correlate to the sliding velocity of thin filaments and its calcium sensitivity in the in vitro motility assay. We suppose that at the level of the molecular ensemble, the cooperative mechanisms prevail in the manifestation of the effects of cardiomyopathy-associated mutations in Tpm. Actin–myosin interaction Tropomyosin Cardiomyopathy mutation Calcium regulation In vitro motility assay Optical trap Shchepkin, Daniil V. aut Nabiev, Salavat R. aut Matyushenko, Alexander M. aut Koubassova, Natalia A. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 40(2019), 3-4 vom: 23. Okt., Seite 299-308 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:40 year:2019 number:3-4 day:23 month:10 pages:299-308 https://doi.org/10.1007/s10974-019-09560-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4219 AR 40 2019 3-4 23 10 299-308 |
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10.1007/s10974-019-09560-8 doi (DE-627)OLC2067131508 (DE-He213)s10974-019-09560-8-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Kopylova, Galina V. verfasserin (orcid)0000-0003-2976-2108 aut Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Nature Switzerland AG 2019 Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on the properties of single actin–myosin interactions and the characteristics of the calcium regulation in an ensemble of myosin molecules immobilised on a glass surface and interacting with regulated thin filaments. Previously, we showed that at saturating $ Ca^{2+} $ concentration the presence of Tpm on the actin filament increases the duration of the interaction. Here, we found that the studied Tpm mutations differently affected the duration: the D175N mutation reduced it compared to WT Tpm, while the E180G mutation increased it. Both dilated mutations made the duration of the interaction even shorter than with F-actin. The duration of the attached state of myosin to the thin filament in the optical trap did not correlate to the sliding velocity of thin filaments and its calcium sensitivity in the in vitro motility assay. We suppose that at the level of the molecular ensemble, the cooperative mechanisms prevail in the manifestation of the effects of cardiomyopathy-associated mutations in Tpm. Actin–myosin interaction Tropomyosin Cardiomyopathy mutation Calcium regulation In vitro motility assay Optical trap Shchepkin, Daniil V. aut Nabiev, Salavat R. aut Matyushenko, Alexander M. aut Koubassova, Natalia A. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 40(2019), 3-4 vom: 23. Okt., Seite 299-308 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:40 year:2019 number:3-4 day:23 month:10 pages:299-308 https://doi.org/10.1007/s10974-019-09560-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4219 AR 40 2019 3-4 23 10 299-308 |
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Kopylova, Galina V. |
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590 570 VZ 12 ssgn BIODIV DE-30 fid Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels Actin–myosin interaction Tropomyosin Cardiomyopathy mutation Calcium regulation In vitro motility assay Optical trap |
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Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels |
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Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels |
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Kopylova, Galina V. |
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Journal of muscle research and cell motility |
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Kopylova, Galina V. Shchepkin, Daniil V. Nabiev, Salavat R. Matyushenko, Alexander M. Koubassova, Natalia A. Levitsky, Dmitrii I. Bershitsky, Sergey Y. |
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cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels |
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Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels |
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Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on the properties of single actin–myosin interactions and the characteristics of the calcium regulation in an ensemble of myosin molecules immobilised on a glass surface and interacting with regulated thin filaments. Previously, we showed that at saturating $ Ca^{2+} $ concentration the presence of Tpm on the actin filament increases the duration of the interaction. Here, we found that the studied Tpm mutations differently affected the duration: the D175N mutation reduced it compared to WT Tpm, while the E180G mutation increased it. Both dilated mutations made the duration of the interaction even shorter than with F-actin. The duration of the attached state of myosin to the thin filament in the optical trap did not correlate to the sliding velocity of thin filaments and its calcium sensitivity in the in vitro motility assay. We suppose that at the level of the molecular ensemble, the cooperative mechanisms prevail in the manifestation of the effects of cardiomyopathy-associated mutations in Tpm. © Springer Nature Switzerland AG 2019 |
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Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on the properties of single actin–myosin interactions and the characteristics of the calcium regulation in an ensemble of myosin molecules immobilised on a glass surface and interacting with regulated thin filaments. Previously, we showed that at saturating $ Ca^{2+} $ concentration the presence of Tpm on the actin filament increases the duration of the interaction. Here, we found that the studied Tpm mutations differently affected the duration: the D175N mutation reduced it compared to WT Tpm, while the E180G mutation increased it. Both dilated mutations made the duration of the interaction even shorter than with F-actin. The duration of the attached state of myosin to the thin filament in the optical trap did not correlate to the sliding velocity of thin filaments and its calcium sensitivity in the in vitro motility assay. We suppose that at the level of the molecular ensemble, the cooperative mechanisms prevail in the manifestation of the effects of cardiomyopathy-associated mutations in Tpm. © Springer Nature Switzerland AG 2019 |
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Abstract In the heart, mutations in the TPM1 gene encoding the α-isoform of tropomyosin lead, in particular, to the development of hypertrophic and dilated cardiomyopathies. We compared the effects of hypertrophic, D175N and E180G, and dilated, E40K and E54K, cardiomyopathy mutations in TPM1 gene on the properties of single actin–myosin interactions and the characteristics of the calcium regulation in an ensemble of myosin molecules immobilised on a glass surface and interacting with regulated thin filaments. Previously, we showed that at saturating $ Ca^{2+} $ concentration the presence of Tpm on the actin filament increases the duration of the interaction. Here, we found that the studied Tpm mutations differently affected the duration: the D175N mutation reduced it compared to WT Tpm, while the E180G mutation increased it. Both dilated mutations made the duration of the interaction even shorter than with F-actin. The duration of the attached state of myosin to the thin filament in the optical trap did not correlate to the sliding velocity of thin filaments and its calcium sensitivity in the in vitro motility assay. We suppose that at the level of the molecular ensemble, the cooperative mechanisms prevail in the manifestation of the effects of cardiomyopathy-associated mutations in Tpm. © Springer Nature Switzerland AG 2019 |
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Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels |
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Shchepkin, Daniil V. Nabiev, Salavat R. Matyushenko, Alexander M. Koubassova, Natalia A. Levitsky, Dmitrii I. Bershitsky, Sergey Y. |
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