期刊
JOURNAL OF PATHOLOGY
卷 227, 期 1, 页码 81-93出版社
WILEY
DOI: 10.1002/path.3982
关键词
desmosomal cadherin; E-cadherin-Src signalling; cell-cell adhesion; epithelial cells; pemphigus vulgaris
资金
- MRC
- Institute of Dentistry
- London School of Medicine and Dentistry
- British Skin Foundation
E-cadherin, a classical cadherin, is an adhesion receptor in adherens junctions and has important functions in cellcell adhesion and cell signalling. Recently we reported that a desmosomal cadherin, desmoglein 3 (Dsg3), an autoantigen in pemphigus vulgaris (PV), associates with E-cadherin and activates Src, which results in tyrosine phosphorylation of adherens junction proteins. However, the nature of such an interaction and its role in cellcell adhesion remain unclear. In this report, we provide direct evidence that it is the detergent-soluble, non-desmosomal Dsg3 that regulates the activity of Src and its association with E-cadherin in adherens junction formation. Modulation of Dsg3 levels, either by Dsg3 silencing or over-expression, alters Src activity and its association with E-cadherin. Dsg3 silencing caused retardation of calcium-induced E-cadherin junction assembly and a reduction of desmosomal protein expression. Furthermore, we provide evidence that this signalling pathway is involved, at least in part, in the pathophysiology of pemphigus. Along with the reduced expression of Dsg3, loss and disruption of E-cadherin and a concomitant decreased pSrc signalling was identified in the basal keratinocytes surrounding the blisters in PV. These findings suggest a novel function for Dsg3 in the control of E-cadherinSrc signalling and cellcell adhesion. Copyright (c) 2012 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
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