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. STKE, 14 February 2006
Vol. 2006, Issue 322, p. tw62
[DOI: 10.1126/stke.3222006tw62]

EDITORS' CHOICE

ALLOSTERIC REGULATION Modulating the Scaffold

Signaling complexes are often pre-assembled into complexes. So-called scaffold proteins help to maintain these complexes and can contribute to specificity in various signaling systems. Bhattacharyya et al. (see the Perspective by Breitkreutz and Tyers) show that the role of such scaffolds can go beyond support and spatial localization. In yeast, mating pheromone causes activation of a series of kinases that all interact with the scaffold protein Ste5, and signal transduction through this pathway activates the mitogen-activated protein kinase Fus3. When Fus 3 binds to Ste5, this interaction causes an allosteric partial activation of Fus3's kinase activity. Fus3 then appears to provide negative feedback in the system by phosphorylating the Ste5 scaffold.

R. P. Bhattacharyya, A. Reményi, M. C. Good, C. J. Bashor, A. M. Falick, W. A. Lim, The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway. Science 311, 822-826 (2006). [Abstract] [Full Text]

A. Breitkreutz, M. Tyers, A sophisticated scaffold wields a new trick. Science 311, 789-790 (2006). [Summary] [Full Text]

Citation: Modulating the Scaffold. Sci. STKE 2006, tw62 (2006).



To Advertise     Find Products


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