期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 26, 页码 7160-7165出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1606272113
关键词
desmosome; cell adhesion; cadherin; heterophilic binding
资金
- NIH [R01 GM062270, R01 GM030518, P41 GM103403]
- NSF [MCB-1412472]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1412472] Funding Source: National Science Foundation
Desmosomes are intercellular adhesive junctions that impart strength to vertebrate tissues. Their dense, ordered intercellular attachments are formed by desmogleins (Dsgs) and desmocollins (Dscs), but the nature of trans-cellular interactions between these specialized cadherins is unclear. Here, using solution biophysics and coated-bead aggregation experiments, we demonstrate family-wise heterophilic specificity: All Dsgs form adhesive dimers with all Dscs, with affinities characteristic of each Dsg: Dsc pair. Crystal structures of ectodomains from Dsg2 and Dsg3 and from Dsc1 and Dsc2 show binding through a strand-swap mechanism similar to that of homophilic classical cadherins. However, conserved charged amino acids inhibit Dsg: Dsg and Dsc: Dsc interactions by same-charge repulsion and promote heterophilic Dsg: Dsc interactions through opposite-charge attraction. These findings show that Dsg: Dsc heterodimers represent the fundamental adhesive unit of desmosomes and provide a structural framework for understanding desmosome assembly.
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