The neural cell adhesion molecule binds to fibroblast growth factor receptor 2

TY - JOUR

T1 - The neural cell adhesion molecule binds to fibroblast growth factor receptor 2

AU - Christensen, Claus

AU - Lauridsen, Jes B

AU - Berezin, Vladimir

AU - Bock, Elisabeth

AU - Kiselyov, Vladislav V

N1 - Keywords: Adenosine Triphosphate; Amino Acid Sequence; Neural Cell Adhesion Molecules; Protein Binding; Receptor, Fibroblast Growth Factor, Type 2; Recombinant Proteins; Surface Plasmon Resonance

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

U2 - 10.1016/j.febslet.2006.05.008

DO - 10.1016/j.febslet.2006.05.008

M3 - Journal article

C2 - 16709412

SN - 0014-5793

VL - 580

SP - 3386

EP - 3390

JO - F E B S Letters

JF - F E B S Letters

IS - 14

ER -