Reactome: A Curated Pathway Database

L1 trans-homophilic interaction

Stable Identifier
R-HSA-374680
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

Interaction with ERM may lead to lateral oligomerization of phosphorylated L1 and this enhances the homophilic trans adhesion of L1.
L1 mediates cell-cell adhesion by a trans-homophilic binding mechanism. In the nonengaged resting state the L1 N-terminal Ig domains adopt a horseshoe like structure due to an intramolecular binding between domains 1 and 4 or 2 and 3, respectively. When engaged in homophilic binding between adjacent cells, L1 could undergo a conformational change leading to a pairwise antiparallel alignment of Ig domains 1-4 and 2-3.

Literature References
Participants
Participant Of
Orthologous Events