Cargando…
Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold
Thy-1/CD90 is a glycoprotein attached to the outer face of the plasma membrane with various functions, which depend on the context of specific physiological or pathological conditions. Many of these reported functions for Thy-1/CD90 arose from studies by our group, which identified the first ligand/...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6689999/ https://www.ncbi.nlm.nih.gov/pubmed/31428610 http://dx.doi.org/10.3389/fcell.2019.00132 |
_version_ | 1783443128619892736 |
---|---|
author | Leyton, Lisette Díaz, Jorge Martínez, Samuel Palacios, Esteban Pérez, Leonardo A. Pérez, Ramón D. |
author_facet | Leyton, Lisette Díaz, Jorge Martínez, Samuel Palacios, Esteban Pérez, Leonardo A. Pérez, Ramón D. |
author_sort | Leyton, Lisette |
collection | PubMed |
description | Thy-1/CD90 is a glycoprotein attached to the outer face of the plasma membrane with various functions, which depend on the context of specific physiological or pathological conditions. Many of these reported functions for Thy-1/CD90 arose from studies by our group, which identified the first ligand/receptor for Thy-1/CD90 as an integrin. This finding initiated studies directed toward unveiling the molecular mechanisms that operate downstream of Thy-1/CD90 activation, and its possible interaction with proteins in the membrane plane to regulate their function. The association of Thy-1/CD90 with a number of cell surface molecules allows the formation of extra/intracellular multiprotein complexes composed of various ligands and receptors, extracellular matrix proteins, intracellular signaling proteins, and the cytoskeleton. The complexes sense changes that occur inside and outside the cells, with Thy-1/CD90 at the core of this extracellular molecular platform. Molecular platforms are scaffold-containing microdomains where key proteins associate to prominently influence cellular processes and behavior. Each component, by itself, is less effective, but when together with various scaffold proteins to form a platform, the components become more specific and efficient to convey the messages. This review article discusses the experimental evidence that supports the role of Thy-1/CD90 as a membrane-associated platform (ThyMAP). |
format | Online Article Text |
id | pubmed-6689999 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-66899992019-08-19 Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold Leyton, Lisette Díaz, Jorge Martínez, Samuel Palacios, Esteban Pérez, Leonardo A. Pérez, Ramón D. Front Cell Dev Biol Cell and Developmental Biology Thy-1/CD90 is a glycoprotein attached to the outer face of the plasma membrane with various functions, which depend on the context of specific physiological or pathological conditions. Many of these reported functions for Thy-1/CD90 arose from studies by our group, which identified the first ligand/receptor for Thy-1/CD90 as an integrin. This finding initiated studies directed toward unveiling the molecular mechanisms that operate downstream of Thy-1/CD90 activation, and its possible interaction with proteins in the membrane plane to regulate their function. The association of Thy-1/CD90 with a number of cell surface molecules allows the formation of extra/intracellular multiprotein complexes composed of various ligands and receptors, extracellular matrix proteins, intracellular signaling proteins, and the cytoskeleton. The complexes sense changes that occur inside and outside the cells, with Thy-1/CD90 at the core of this extracellular molecular platform. Molecular platforms are scaffold-containing microdomains where key proteins associate to prominently influence cellular processes and behavior. Each component, by itself, is less effective, but when together with various scaffold proteins to form a platform, the components become more specific and efficient to convey the messages. This review article discusses the experimental evidence that supports the role of Thy-1/CD90 as a membrane-associated platform (ThyMAP). Frontiers Media S.A. 2019-07-26 /pmc/articles/PMC6689999/ /pubmed/31428610 http://dx.doi.org/10.3389/fcell.2019.00132 Text en Copyright © 2019 Leyton, Díaz, Martínez, Palacios, Pérez and Pérez. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Cell and Developmental Biology Leyton, Lisette Díaz, Jorge Martínez, Samuel Palacios, Esteban Pérez, Leonardo A. Pérez, Ramón D. Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold |
title | Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold |
title_full | Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold |
title_fullStr | Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold |
title_full_unstemmed | Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold |
title_short | Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold |
title_sort | thy-1/cd90 a bidirectional and lateral signaling scaffold |
topic | Cell and Developmental Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6689999/ https://www.ncbi.nlm.nih.gov/pubmed/31428610 http://dx.doi.org/10.3389/fcell.2019.00132 |
work_keys_str_mv | AT leytonlisette thy1cd90abidirectionalandlateralsignalingscaffold AT diazjorge thy1cd90abidirectionalandlateralsignalingscaffold AT martinezsamuel thy1cd90abidirectionalandlateralsignalingscaffold AT palaciosesteban thy1cd90abidirectionalandlateralsignalingscaffold AT perezleonardoa thy1cd90abidirectionalandlateralsignalingscaffold AT perezramond thy1cd90abidirectionalandlateralsignalingscaffold |