Long-Tailed Unconventional Class I Myosins in Health and Disease
Long-tailed unconventional class I myosin, Myosin 1E (MYO1E) and Myosin 1F (MYO1F) are motor proteins that use chemical energy from the hydrolysis of adenosine triphosphate (ATP) to produce mechanical work along the actin cytoskeleton. On the basis of their motor properties and structural features,...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-04-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/7/2555 |
| _version_ | 1797571280100130816 |
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| author | A. Navinés-Ferrer M. Martín |
| author_facet | A. Navinés-Ferrer M. Martín |
| author_sort | A. Navinés-Ferrer |
| collection | DOAJ |
| description | Long-tailed unconventional class I myosin, Myosin 1E (MYO1E) and Myosin 1F (MYO1F) are motor proteins that use chemical energy from the hydrolysis of adenosine triphosphate (ATP) to produce mechanical work along the actin cytoskeleton. On the basis of their motor properties and structural features, myosins perform a variety of essential roles in physiological processes such as endocytosis, exocytosis, cell adhesion, and migration. The long tailed unconventional class I myosins are characterized by having a conserved motor head domain, which binds actin and hydrolyzes ATP, followed by a short neck with an isoleucine-glutamine (IQ) motif, which binds calmodulin and is sensitive to calcium, and a tail that contains a pleckstrin homology domain (PH), a tail homology 1 domain (TH1), wherein these domains allow membrane binding, a tail homology 2 domain (TH2), an ATP-insensitive actin-binding site domain, and a single Src homology 3 domain (SH3) susceptible to binding proline rich regions in other proteins. Therefore, these motor proteins are able to bind actin, plasma membrane, and other molecules (adaptor, kinases, membrane proteins) that contribute to their function, ranging from increasing membrane tension to molecular trafficking and cellular adhesion. MYO1E and MYO1F function in host self-defense, with a better defined role in innate immunity in cell migration and phagocytosis. Impairments of their function have been identified in patients suffering pathologies ranging from tumoral processes to kidney diseases. In this review, we summarize our current knowledge of specific features and functions of MYO1E and MYO1F in various tissues, as well as their involvement in disease. |
| first_indexed | 2024-03-10T20:38:05Z |
| format | Article |
| id | doaj.art-baaf669271184079abece122cb62c7d6 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T20:38:05Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-baaf669271184079abece122cb62c7d62023-11-19T20:53:58ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-04-01217255510.3390/ijms21072555Long-Tailed Unconventional Class I Myosins in Health and DiseaseA. Navinés-Ferrer0M. Martín1Biochemistry and Molecular Biology Unit, Biomedicine Department, Faculty of Medicine, University of Barcelona, 08036 Barcelona, SpainBiochemistry and Molecular Biology Unit, Biomedicine Department, Faculty of Medicine, University of Barcelona, 08036 Barcelona, SpainLong-tailed unconventional class I myosin, Myosin 1E (MYO1E) and Myosin 1F (MYO1F) are motor proteins that use chemical energy from the hydrolysis of adenosine triphosphate (ATP) to produce mechanical work along the actin cytoskeleton. On the basis of their motor properties and structural features, myosins perform a variety of essential roles in physiological processes such as endocytosis, exocytosis, cell adhesion, and migration. The long tailed unconventional class I myosins are characterized by having a conserved motor head domain, which binds actin and hydrolyzes ATP, followed by a short neck with an isoleucine-glutamine (IQ) motif, which binds calmodulin and is sensitive to calcium, and a tail that contains a pleckstrin homology domain (PH), a tail homology 1 domain (TH1), wherein these domains allow membrane binding, a tail homology 2 domain (TH2), an ATP-insensitive actin-binding site domain, and a single Src homology 3 domain (SH3) susceptible to binding proline rich regions in other proteins. Therefore, these motor proteins are able to bind actin, plasma membrane, and other molecules (adaptor, kinases, membrane proteins) that contribute to their function, ranging from increasing membrane tension to molecular trafficking and cellular adhesion. MYO1E and MYO1F function in host self-defense, with a better defined role in innate immunity in cell migration and phagocytosis. Impairments of their function have been identified in patients suffering pathologies ranging from tumoral processes to kidney diseases. In this review, we summarize our current knowledge of specific features and functions of MYO1E and MYO1F in various tissues, as well as their involvement in disease.https://www.mdpi.com/1422-0067/21/7/2555unconventional myosinsintegrinsadaptor moleculesimmune cellscell adhesionmigration |
| spellingShingle | A. Navinés-Ferrer M. Martín Long-Tailed Unconventional Class I Myosins in Health and Disease International Journal of Molecular Sciences unconventional myosins integrins adaptor molecules immune cells cell adhesion migration |
| title | Long-Tailed Unconventional Class I Myosins in Health and Disease |
| title_full | Long-Tailed Unconventional Class I Myosins in Health and Disease |
| title_fullStr | Long-Tailed Unconventional Class I Myosins in Health and Disease |
| title_full_unstemmed | Long-Tailed Unconventional Class I Myosins in Health and Disease |
| title_short | Long-Tailed Unconventional Class I Myosins in Health and Disease |
| title_sort | long tailed unconventional class i myosins in health and disease |
| topic | unconventional myosins integrins adaptor molecules immune cells cell adhesion migration |
| url | https://www.mdpi.com/1422-0067/21/7/2555 |
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