A guide and guard: The many faces of T-cadherin

Maria Philippova, Manjunath B. Joshi, Emmanouil Kyriakakis, Dennis Pfaff, Paul Erne, Therese J. Resink

Research output: Contribution to journalReview article

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Abstract

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.

Original languageEnglish
Pages (from-to)1035-1044
Number of pages10
JournalCellular Signalling
Volume21
Issue number7
DOIs
Publication statusPublished - 07-2009

All Science Journal Classification (ASJC) codes

  • Cell Biology

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    Philippova, M., Joshi, M. B., Kyriakakis, E., Pfaff, D., Erne, P., & Resink, T. J. (2009). A guide and guard: The many faces of T-cadherin. Cellular Signalling, 21(7), 1035-1044. https://doi.org/10.1016/j.cellsig.2009.01.035