Reactome: A Curated Pathway Database
THIS SITE IS USED FOR CURATION AND TESTING
IT IS NOT STABLE, IS LINKED TO AN INCOMPLETE DATA SET, AND IS NOT MONITORED FOR PERFORMANCE. WE STRONGLY RECOMMEND THE USE OF OUR PUBLIC SITE

Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Name Email address

Details on Person CDH1 (E-cadherin) forms a homotypic trans-complex with CDH1 ...

Class:IdSummation:9934421
_displayNameCDH1 (E-cadherin) forms a homotypic trans-complex with CDH1 ...
_timestamp2025-12-01 16:54:17
created[InstanceEdit:9934419] Orlic-Milacic, Marija, 2025-01-08
literatureReference[LiteratureReference:9762154] Adhesive but not lateral E-cadherin complexes require calcium and catenins for their formation
[LiteratureReference:201971] Structural basis of calcium-induced E-cadherin rigidification and dimerization
[LiteratureReference:9934425] Calcium binding and homoassociation of E-cadherin domains
[LiteratureReference:9934437] Actin-delimited adhesion-independent clustering of E-cadherin forms the nanoscale building blocks of adherens junctions
[LiteratureReference:9934434] Dynamics and functions of E-cadherin complexes in epithelial cell and tissue morphogenesis
modified[InstanceEdit:9934429] Orlic-Milacic, Marija, 2025-01-08
[InstanceEdit:9934433] Orlic-Milacic, Marija, 2025-01-08
[InstanceEdit:9934443] Orlic-Milacic, Marija, 2025-01-08
[InstanceEdit:9934512] Orlic-Milacic, Marija, 2025-01-08
[InstanceEdit:9936230] Orlic-Milacic, Marija, 2025-01-22
[InstanceEdit:9975419] Orlic-Milacic, Marija, 2025-12-01
textCDH1 (E-cadherin) forms a homotypic trans-complex with CDH1 molecules presented on the plasma membrane of a neighbouring cell, where two CDH1 molecules interact through their extracellular domains in a calcium (Ca2+)-dependent, and catenin-dependent manner (Chitaev and Troyanovski 1998). Based on a structural study using the extracellular domain of the mouse CDH1, it was determined that twelve Ca2+ ions per CDH1 molecule were needed for homotypic dimerization (Nagar et al. 1996). Another study with the mouse CDH1 reported that nine Ca2+ ions per CDH1 molecule were sufficient for homotypic dimerization (Koch et al. 1997). Using super-resolution microscopy techniques it was found that loosely organized cis-clusters of approximately five CDH1 molecules serve as the precursors of trans-ligated adhesive clusters, consisting of homotypic trans-dimers, that make up the adherens junction (Wu et al. 2015; reviewed in Zhang et al. 2023). CDH1 clusters in both interacting cells are surrounded by the cytosolic F-actin meshwork, but the F-actin meshwork is not necessary for the establishment of homotypic trans-interactions (Wu et al. 2015).
(summation)[Reaction:9934410] CDH1 forms homotypic trans-dimers [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by CDH1 (E-cadherin) forms a homotypic trans-complex with CDH1 ... (9934421)