Thy-1, a Pathfinder Protein for the Post-genomic Era

Thy-1 is possibly the smallest of cell surface proteins – 110 amino acids folded into an Immunoglobulin variable domain, tethered to the outer leaflet of the cell surface membrane via just the two saturated fatty acids of its glycosylphosphatidylinositol (GPI) anchor. Yet Thy-1 is emerging as a key...

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Main Author: Roger J. Morris
Format: Article
Language:English
Published: Frontiers Media S.A. 2018-12-01
Series:Frontiers in Cell and Developmental Biology
Subjects:
Online Access:https://www.frontiersin.org/article/10.3389/fcell.2018.00173/full
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author Roger J. Morris
author_facet Roger J. Morris
author_sort Roger J. Morris
collection DOAJ
description Thy-1 is possibly the smallest of cell surface proteins – 110 amino acids folded into an Immunoglobulin variable domain, tethered to the outer leaflet of the cell surface membrane via just the two saturated fatty acids of its glycosylphosphatidylinositol (GPI) anchor. Yet Thy-1 is emerging as a key regulator of differentiation in cells of endodermal, mesodermal, and ectodermal origin, acting as both a ligand (for certain integrins and other receptors), and as a receptor, able to modulate signaling and hence differentiation in the Thy-1-expressing cell. This is an extraordinary diversity of molecular pathways to be controlled by a molecule that does not even cross the cell membrane. Here I review aspects of the cell biology of Thy-1, and studies of its role as deduced from gene knock-out studies, that suggest how this protein can participate in so many different signaling-related functions. While mechanisms differ in molecular detail, it appears overall that Thy-1 dampens down signaling to control function.
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spelling doaj.art-6124c85f867b445396054299584b88bd2022-12-22T01:28:44ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2018-12-01610.3389/fcell.2018.00173428892Thy-1, a Pathfinder Protein for the Post-genomic EraRoger J. MorrisThy-1 is possibly the smallest of cell surface proteins – 110 amino acids folded into an Immunoglobulin variable domain, tethered to the outer leaflet of the cell surface membrane via just the two saturated fatty acids of its glycosylphosphatidylinositol (GPI) anchor. Yet Thy-1 is emerging as a key regulator of differentiation in cells of endodermal, mesodermal, and ectodermal origin, acting as both a ligand (for certain integrins and other receptors), and as a receptor, able to modulate signaling and hence differentiation in the Thy-1-expressing cell. This is an extraordinary diversity of molecular pathways to be controlled by a molecule that does not even cross the cell membrane. Here I review aspects of the cell biology of Thy-1, and studies of its role as deduced from gene knock-out studies, that suggest how this protein can participate in so many different signaling-related functions. While mechanisms differ in molecular detail, it appears overall that Thy-1 dampens down signaling to control function.https://www.frontiersin.org/article/10.3389/fcell.2018.00173/fullmembrane proteinGPI (glycosylphosphatidylinositol)adhesionsignaling systemmutant miceneuron
spellingShingle Roger J. Morris
Thy-1, a Pathfinder Protein for the Post-genomic Era
Frontiers in Cell and Developmental Biology
membrane protein
GPI (glycosylphosphatidylinositol)
adhesion
signaling system
mutant mice
neuron
title Thy-1, a Pathfinder Protein for the Post-genomic Era
title_full Thy-1, a Pathfinder Protein for the Post-genomic Era
title_fullStr Thy-1, a Pathfinder Protein for the Post-genomic Era
title_full_unstemmed Thy-1, a Pathfinder Protein for the Post-genomic Era
title_short Thy-1, a Pathfinder Protein for the Post-genomic Era
title_sort thy 1 a pathfinder protein for the post genomic era
topic membrane protein
GPI (glycosylphosphatidylinositol)
adhesion
signaling system
mutant mice
neuron
url https://www.frontiersin.org/article/10.3389/fcell.2018.00173/full
work_keys_str_mv AT rogerjmorris thy1apathfinderproteinforthepostgenomicera