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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Detalles Bibliográficos
Autores: Navinés Ferrer, Arnau, Martín Andorrà, Margarita
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/162464
Acceso en línea:https://hdl.handle.net/2445/162464
Access Level:acceso abierto
Palabra clave:Proteïnes portadores
Migració cel·lular
Càncer
Carrier proteins
Cell migration
Cancer
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spelling Long-Tailed Unconventional Class I Myosins in Health and DiseaseNavinés Ferrer, ArnauMartín Andorrà, MargaritaProteïnes portadoresMigració cel·lularCàncerCarrier proteinsCell migrationCancerLong-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.MDPI2020202020202020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion13 p.application/pdfhttps://hdl.handle.net/2445/162464Articles publicats en revistes (Biomedicina)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.3390/ijms21072555International Journal of Molecular Sciences, 2020, vol. 21, num. 7, p. 2555https://doi.org/10.3390/ijms21072555cc-by (c) Navinés Ferrer, Arnau et al., 2020http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:recercat.cat:2445/1624642026-05-29T05:05:01Z
dc.title.none.fl_str_mv Long-Tailed Unconventional Class I Myosins in Health and Disease
title Long-Tailed Unconventional Class I Myosins in Health and Disease
spellingShingle Long-Tailed Unconventional Class I Myosins in Health and Disease
Navinés Ferrer, Arnau
Proteïnes portadores
Migració cel·lular
Càncer
Carrier proteins
Cell migration
Cancer
title_short 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_sort Long-Tailed Unconventional Class I Myosins in Health and Disease
dc.creator.none.fl_str_mv Navinés Ferrer, Arnau
Martín Andorrà, Margarita
author Navinés Ferrer, Arnau
author_facet Navinés Ferrer, Arnau
Martín Andorrà, Margarita
author_role author
author2 Martín Andorrà, Margarita
author2_role author
dc.subject.none.fl_str_mv Proteïnes portadores
Migració cel·lular
Càncer
Carrier proteins
Cell migration
Cancer
topic Proteïnes portadores
Migració cel·lular
Càncer
Carrier proteins
Cell migration
Cancer
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.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/162464
url https://hdl.handle.net/2445/162464
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/ijms21072555
International Journal of Molecular Sciences, 2020, vol. 21, num. 7, p. 2555
https://doi.org/10.3390/ijms21072555
dc.rights.none.fl_str_mv cc-by (c) Navinés Ferrer, Arnau et al., 2020
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Navinés Ferrer, Arnau et al., 2020
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 13 p.
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Biomedicina)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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