Thy-1/CD90 a Bidirectional and Lateral Signaling Scaffold

• Published in: Frontiers in cell and developmental biology 2019-07, Vol.7, p.132-132
• Main Authors: Leyton, Lisette, Díaz, Jorge, Martínez, Samuel, Palacios, Esteban, Pérez, Leonardo A, Pérez, Ramón D
• Format: Article
• Language: English
• Subjects: Cell and Developmental Biology; GPI-anchor; integrin; membrane-associated; PLATFORM; syndecan 4; Thy-1 (CD90)
• ISSN: 2296-634X; 2296-634X
• DOI: 10.3389/fcell.2019.00132

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).