Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. Signal., 17 February 2009
Vol. 2, Issue 58, p. ra6
[DOI: 10.1126/scisignal.2000021]

RESEARCH

Editor's Summary

Is Timing Everything?
Five tyrosine residues in the tyrosine kinase domain of fibroblast growth factor receptor 1 (FGFR1) undergo autophosphorylation, a process that both enhances its kinase activity and provides binding sites for downstream signaling molecules. Lew et al. investigated the mechanisms underlying this sequential and precisely ordered autophosphorylation and determined that it was under kinetic control, with the order of phosphorylation depending on the location of individual tyrosines within the primary and tertiary structures of the FGFR1 kinase domain. Intriguingly, the order in which these tyrosine residues underwent autophosphorylation was disrupted by a glioblastoma-derived, oncogenic FGFR1 point mutation. The authors postulate that such mutations may also alter the temporal recruitment of downstream signaling molecules and this may contribute to their oncogenic activity.

Citation: E. D. Lew, C. M. Furdui, K. S. Anderson, J. Schlessinger, The Precise Sequence of FGF Receptor Autophosphorylation Is Kinetically Driven and Is Disrupted by Oncogenic Mutations. Sci. Signal. 2, ra6 (2009).

Read the Full Text

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Science Signaling Podcast: 03 March 2009.
J. Schlessinger and A. M. VanHook (2009)
Science Signaling 2, pc5
   Abstract »    Full Text »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882