Reactome | L1 trans-homophilic interaction

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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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

PubMed ID	Title	Journal	Year
9721721	Identification of a homophilic binding site in immunoglobulin-like domain 2 of the cell adhesion molecule L1 Zhao, X, Yip, PM, Siu, CH	J Neurochem	1998
19278660	Cryo-electron tomography of homophilic adhesion mediated by the neural cell adhesion molecule L1 He, Y, Jensen, GJ, Bjorkman, PJ	Structure	2009
2448316	Neuron-glia cell adhesion molecule interacts with neurons and astroglia via different binding mechanisms Grumet, M, Edelman, GM	J Cell Biol	1988
7493978	Colocalization of the homophilic binding site and the neuritogenic activity of the cell adhesion molecule L1 to its second Ig-like domain Zhao, X, Siu, CH	J Biol Chem	1995