L1 interaction with Integrins

Stable Identifier
Reaction [binding]
Homo sapiens
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L1 can function as a trans-heterophilic ligand for multiple members of the integrin superfamily. It binds multiple integrins including alphavbeta3, alphavbeta1, alpha5beta1, alphaIIbbeta3 and alpha9beta 1. The RGD motif in the sixth Ig domain and the third FnIII repeat of L1 are important for these interactions, which serves to strengthen the adhesion of the neuron to the extracellular matrix.
L1 and beta1 integrins association activates a common intracellular signaling pathway. This pathway involves the sequential activation of the tyrosine kinase c-Src, PI3 kinase, Vav2 guanine nucleotide exchange factor, Rac1 GTPase, PAK1, MEK, and the MAP kinases ERK1/2, which is essential for L1 induced neurite outgrowth and cell motility.
Literature References
PubMed ID Title Journal Year
9396761 A single immunoglobulin-like domain of the human neural cell adhesion molecule L1 supports adhesion by multiple vascular and platelet integrins

Montgomery, AM, Siu, CH, Silletti, S, Ginsberg, MH, Cheresh, DA, Brooks, PC, Yip, PM, Felding-Habermann, B, Mei, F, O'Toole, TE

J Cell Biol 1997
18555990 The RGD integrin binding site in human L1-CAM is important for nuclear signaling

Müerköster, SS, Kiefel, H, Riedle, S, Altevogt, P, Gast, D, Schäfer, H, Schäfer, MK

Exp Cell Res 2008
Orthologous Events
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