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Structural basis for a direct interaction between FGFR1 and NCAM and evidence for a regulatory role of ATP.

Authors: Kiselyov, VV  Skladchikova, G  Hinsby, AM  Jensen, PH  Kulahin, N  Soroka, V  Pedersen, N  Tsetlin, V  Poulsen, FM  Berezin, V  Bock, E 
Citation: Kiselyov VV, etal., Structure (Camb) 2003 Jun;11(6):691-701.
Pubmed: (View Article at PubMed) PMID:12791257

The neural cell adhesion molecule (NCAM) promotes axonal outgrowth, presumably through an interaction with the fibroblast growth factor receptor (FGFR). NCAM also has a little-understood ATPase activity. We here demonstrate for the first time a direct interaction between NCAM (fibronectin type III [F3] modules 1 and 2) and FGFR1 (Ig modules 2 and 3) by surface plasmon resonance (SPR) analysis. The structure of the NCAM F3 module 2 was determined by NMR and the module was shown by NMR to interact with the FGFR1 Ig module 3 and ATP. The NCAM sites binding to FGFR and ATP were found to overlap and ATP was shown by SPR to inhibit the NCAM-FGFR binding, indicating that ATP probably regulates the NCAM-FGFR interaction. Furthermore, we demonstrate that the NCAM module was able to induce activation (phosphorylation) of FGFR and to stimulate neurite outgrowth. In contrast, ATP inhibited neurite outgrowth induced by the module.

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CRRD Object Information
CRRD ID: 1358297
Created: 2005-06-08
Species: All species
Last Modified: 2005-06-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.