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Review

Long-Tailed Unconventional Class I Myosins in Health and Disease

by 1,2 and 1,2,3,*
1
Biochemistry and Molecular Biology Unit, Biomedicine Department, Faculty of Medicine, University of Barcelona, 08036 Barcelona, Spain
2
Laboratory of Clinic and Experimental Respiratory Immunoallergy, IDIBAPS, 08036 Barcelona, Spain
3
ARADyAL research network, Carlos III Health Institute, 28029 Madrid, Spain
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(7), 2555; https://doi.org/10.3390/ijms21072555
Received: 27 February 2020 / Revised: 3 April 2020 / Accepted: 4 April 2020 / Published: 7 April 2020
(This article belongs to the Special Issue Cell Adhesion and Migration in Health and Diseases)
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. View Full-Text
Keywords: unconventional myosins; integrins; adaptor molecules; immune cells; cell adhesion; migration; phagocytosis; host defense; cancer unconventional myosins; integrins; adaptor molecules; immune cells; cell adhesion; migration; phagocytosis; host defense; cancer
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MDPI and ACS Style

Navinés-Ferrer, A.; Martín, M. Long-Tailed Unconventional Class I Myosins in Health and Disease. Int. J. Mol. Sci. 2020, 21, 2555. https://doi.org/10.3390/ijms21072555

AMA Style

Navinés-Ferrer A, Martín M. Long-Tailed Unconventional Class I Myosins in Health and Disease. International Journal of Molecular Sciences. 2020; 21(7):2555. https://doi.org/10.3390/ijms21072555

Chicago/Turabian Style

Navinés-Ferrer, A.; Martín, M. 2020. "Long-Tailed Unconventional Class I Myosins in Health and Disease" Int. J. Mol. Sci. 21, no. 7: 2555. https://doi.org/10.3390/ijms21072555

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