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Cited by 344

The DOI matches its Crossref record; 91 of the 91 references it cites were found in a registry or an index.

Thinking outside the cell: how cadherins drive adhesion

Open access
Brasch, Julia, Harrison, Oliver J., Honig, Barry, Shapiro, Lawrence·2012·Trends in Cell Biology
DOI 10.1016/j.tcb.2012.03.004
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Abstract

Cadherins embody a superfamily of cell-surface glycoproteins whose ectodomains contain multiple repeats of β-sandwich EC (extracellular cadherin) domains that adopt a similar fold to immunoglobulin domains. The best characterized cadherins are the vertebrate “classical” cadherins, which mediate adhesion via trans homodimerization between their membrane-distal EC1 domains that extend from apposed cells, and assemble intercellular adherens junctions through cis clustering. To form mature trans adhesive dimers, cadherin domains from apposed cells dimerize in a “strand-swapped” conformation. This occurs in a two-step binding process involving a fast-binding intermediate called the “X-dimer”. Trans dimers are less flexible than cadherin monomers, a factor which drives junction assembly following cell-cell contact by reducing the entropic cost associated with the formation of lateral cis oligomers. Cadherins outside of the classical subfamily appear to have evolved distinct adhesive mechanisms which are just now beginning to be understood.

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Show all 91 references

Research works printed but not linked: 5

  1. Vunnam, 2011, Prolines in betaA-sheet of neural cadherin act as a switch to control the dynamics of the equilibrium between monomer and dimer, Biochemistry, 50, 6959, 10.1021/bi2007788 · doi:10.1021/bi2007788
  2. Uehara, 2006, Distribution of adherens junction mediated by VE-cadherin complex in rat spleen sinus endothelial cells, Cell Tissue Res., 323, 417, 10.1007/s00441-005-0064-5 · doi:10.1007/s00441-005-0064-5
  3. Kiener, 2006, The cadherin-11 cytoplasmic juxtamembrane domain promotes alpha-catenin turnover at adherens junctions and intercellular motility, Mol. Biol. Cell, 17, 2366, 10.1091/mbc.E05-08-0745 · doi:10.1091/mbc.e05-08-0745
  4. Jin, 2011, Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca2+-free interdomain linkers, Proc. Natl. Acad. Sci. U.S.A., 109, E127, 10.1073/pnas.1117538108 · doi:10.1073/pnas.1117538108
  5. Troyanovsky, 2003, Adhesive and lateral E-cadherin dimers are mediated by the same interface, Mol. Cell. Biol., 23, 7965, 10.1128/MCB.23.22.7965-7972.2003 · DOI

Cited by

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Metadata

Authors
Brasch, J., Harrison, O. J., Honig, B., & Shapiro, L.
Venue
Trends in Cell Biology
Publisher
Elsevier BV
Published
2012-06
Volume
22
Issue
6
Pages
299-310
ISSN
0962-8924 (ISSN-L)
DOI
10.1016/j.tcb.2012.03.004
OpenAlex
W2089368828
Cited by
344
References
91
FWCI
4.21
Type
journal article
Language
en
Open access
green
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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CoChat. (2026). Citation check: Thinking outside the cell: how cadherins drive adhesion. https://app.cochat.ai/papers/10.1016/j.tcb.2012.03.004
The paper
Brasch, J., Harrison, O. J., Honig, B., & Shapiro, L. (2012). Thinking outside the cell: how cadherins drive adhesion. Trends in Cell Biology. https://doi.org/10.1016/j.tcb.2012.03.004

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.