Abstract
The glycosylphosphatidylinositol (GPI) anchored glycoprotein Thy-1 has been prevalently expressed on the surface of various cell types. The biological function of Thy-1 ranges from T cell activation, cell adhesion, neurite growth, differentiation, metastasis and fibrogenesis and has been extensively reviewed elsewhere. However, current discoveries implicate Thy-1 also functions as a key mechanotransduction mediator. In this review, we will be focusing on the role of Thy-1 in translating extracellular mechanic cues into intracellular biological cascades. The mechanotransduction capability of Thy-1 relies on trans and cis interaction between Thy-1 and RGD-binding integrins; and will be discussed in depth in the review.
Highlights
The glycosylphosphatidylinositol (GPI) anchored glycoprotein Thy-1 has been prevalently expressed on the surface of various cell types
Another study later discovered that this trans interaction between Thy-1 and integrin αvβ3 induces Thy-1 microclustering and colocalization with Cskbinding protein (CBP) while displacing Src kinase from these clusters at the same time (Maldonado et al, 2017)
Integrin mediated mechanotransduction relies on extracellular matrix (ECM) ligand engagement and subsequent integrin clustering, which leads to self-activation of FAK and Src, resulting in downstream RhoA activation and cellular contractility (Hu and Luo, 2013)
Summary
The glycosylphosphatidylinositol (GPI) anchored glycoprotein Thy-1 has been prevalently expressed on the surface of various cell types. Potential interactions between Thy-1 and integrin αvβ5 has been proposed as the mechanism of Thy-1 mediated signaling that blocks activation of TGF-β (Herrera-Molina et al, 2013). The interaction is mediated through the RLD motif on the recombinant Thy-1-FC molecule and the engagement between Thy-1 and αvβ3 can promote focal adhesion formation as well as FAK phosphorylation.
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