L1 trans-homophilic interaction

Stable Identifier
R-HSA-374680
Type
Reaction [binding]
Species
Homo sapiens
Compartment
plasma membrane
ReviewStatus
5/5
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L1 trans-homophilic interaction
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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
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Entity On Other Cell
Participates
as an event of
Orthologous Events
L1 trans-homophilic interaction (Caenorhabditis elegans)
L1 trans-homophilic interaction (Mus musculus)
L1 trans-homophilic interaction (Rattus norvegicus)
L1 trans-homophilic interaction (Xenopus tropicalis)
Authored
Garapati, P V  (2008-07-30)
Reviewed
Maness, PF  (2010-02-16)
Created
Garapati, P V  (2008-07-30)
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