L1-FGFR cis-heterodimerization

Stable Identifier
Reaction [binding]
Homo sapiens
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L1-L1 trans-homodimers interact with the fibroblast growth factor receptor (FGFR). The CAM homology domain (CHD) in the FGFR, which resides between Ig like domains 1 and 2, interacts with the putative FGFR-CHD binding motif in the Fn3 module 4 of L1. This interaction leads to activation of the tyrosine kinase domain of the FGFR and subsequent activation of PLCgamma. PLCgamma then hydrolyses PIP2 to generate IP3 and DAG which finally leads to an increase in localized Ca+2 influx and activation of Ca+2/Calmodulin kinase II.

Literature References
PubMed ID Title Journal Year
18222703 Fibronectin type III (FN3) modules of the neuronal cell adhesion molecule L1 interact directly with the fibroblast growth factor (FGF) receptor

Kulahin, N, Li, S, Hinsby, A, Kiselyov, V, Berezin, V, Bock, E

Mol Cell Neurosci 2008
Participant Of
Orthologous Events
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