There will be a maintenance on OICR IT systems starting Friday Dec 15 at 6PM EST until midnight Sunday Dec 17; Reactome will be affected by this downtime

Service under maintenance from Friday Dec 15 at 6PM EST until midnight Sunday Dec 17

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.

Participants
Participant Of
Orthologous Events