The neural cell adhesion molecule binds to fibroblast growth factor receptor 2.
The neural cell adhesion molecule (NCAM) can bind to and activate fibroblast growth factor receptor 1 (FGFR1). However, there are four major FGFR isoforms (FGFR1-FGFR4), and it is not known whether NCAM also interacts directly with the other three FGFR isoforms. In this study, we show by surface plasmon resonance analysis that NCAM can bind to FGFR2 with an affinity similar to that for the NCAM-FGFR1 interaction. However, the kinetic parameters for the NCAM-FGFR2 binding are different from those of the NCAM-FGFR1 binding. Both receptors were shown to cycle relatively fast between the NCAM bound and unbound states, although FGFR2 cycling was clearly faster (13 times) than the FGFR1 cycling. Moreover, ATP was more effective in inhibiting the binding of NCAM to FGFR1 than to FGFR2, indicating that the binding sites in NCAM for the two receptors are similar, but not identical.
Christensen
Claus
C
Protein Laboratory, Copenhagen University, Denmark.
Lauridsen
Jes B
JB
Berezin
Vladimir
V
Bock
Elisabeth
E
Kiselyov
Vladislav V
VV
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D019006:Neural Cell Adhesion Molecules / Q000378:metabolism*; D011485:Protein Binding; D051497:Receptor, Fibroblast Growth Factor, Type 2 / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D020349:Surface Plasmon Resonance
D019006:Neural Cell Adhesion Molecules; D011994:Recombinant Proteins; D000255:Adenosine Triphosphate; D051497:Receptor, Fibroblast Growth Factor, Type 2