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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Tariq, Humera Rouhi, Mansour Nie, Zhuxiang Jowitt, Thomas A. Tabernero, Lydia Bella, Jordi Baldock, Clair Garrod, David Holmes, David F. |
| Description | Author Affiliation: Tariq H ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.); Bella J ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.); Jowitt TA ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.); Holmes DF ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.); Rouhi M ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.); Nie Z ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.); Baldock C ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.); Garrod D ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.); Tabernero L ( Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom Lydia.Tabernero@manchester.ac.uk.); |
| Abstract | Desmosomes and adherens junctions are intercellular adhesive structures essential for the development and integrity of vertebrate tissue, including the epidermis and heart. Their cell adhesion molecules are cadherins: type 1 cadherins in adherens junctions and desmosomal cadherins in desmosomes. A fundamental difference is that desmosomes have a highly ordered structure in their extracellular region and exhibit calcium-independent hyperadhesion, whereas adherens junctions appear to lack such ordered arrays, and their adhesion is always calcium-dependent. We present here the structure of the entire ectodomain of desmosomal cadherin desmoglein 2 (Dsg2), using a combination of small-angle X-ray scattering, electron microscopy, and solution-based biophysical techniques. This structure reveals that the ectodomain of Dsg2 is flexible even in the calcium-bound state and, on average, is shorter than the type 1 cadherin crystal structures. The Dsg2 structure has an excellent fit with the electron tomography reconstructions of human desmosomes. This fit suggests an arrangement in which desmosomal cadherins form trans interactions but are too far apart to interact in cis, in agreement with previously reported observations. Cadherin flexibility may be key to explaining the plasticity of desmosomes that maintain tissue integrity in their hyperadhesive form, but can adopt a weaker, calcium-dependent adhesion during wound healing and early development. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 17 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adherens Junctions Chemistry Desmoglein 2 Desmosomes Genetics Metabolism Animals CHO Cells Cricetinae Cricetulus Crystallography, X-Ray Protein Structure, Tertiary Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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