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A guide and guard: The many faces of T-cadherin
Cadherins are a superfamily of transmembrane proteins that mediate calcium-dependent intercellular adhesion. T-cadherin (T-cad, H-cadherin or cadherin-13) is an atypical member, lacking transmembrane and cytosolic domains and possessing a glycosylphosphatidylinositol moiety that anchors T-cadherin t...
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Published in: | Cellular signalling 2009-07, Vol.21 (7), p.1035-1044 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Cadherins are a superfamily of transmembrane proteins that mediate calcium-dependent intercellular adhesion. T-cadherin (T-cad, H-cadherin or cadherin-13) is an atypical member, lacking transmembrane and cytosolic domains and possessing a glycosylphosphatidylinositol moiety that anchors T-cadherin to the plasma membrane. This article reviews current knowledge on the biomolecular characteristics of T-cadherin, its expression and function in different tissues in health and disease and its mechanisms of signal transduction. The structural characteristics of T-cadherin protein predict that it is unlikely to function as a “true” adhesion molecule
in vivo. Studies from different fields suggest that it may act rather as a signalling receptor participating in recognition of the environment and regulation of cell motility, proliferation and phenotype. Cellular expression levels of T-cadherin in various tissues frequently correlate (be it negatively or positively) with the proliferative potential of the cells. Loss- and gain-of-function studies demonstrate the ability of T-cadherin to modulate cell motility and growth. Gathering evidence suggests that the “functional predestination” of T-cadherin is in control of tissue architecture through “guiding” navigation of moving structures, segregating functional tissue compartments and “guarding” integrity of functionally connected tissue layers. |
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ISSN: | 0898-6568 1873-3913 |
DOI: | 10.1016/j.cellsig.2009.01.035 |