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Published February 18, 2009 | public
Journal Article

Biochemistry on a Leash: The Roles of Tether Length and Geometry in Signal Integration Proteins

Abstract

We use statistical mechanics and simple ideas from polymer physics to develop a quantitative model of proteins whose activity is controlled by flexibly tethered ligands and receptors. We predict how the properties of tethers influence the function of these proteins and demonstrate how their tether length dependence can be exploited to construct proteins whose integration of multiple signals can be tuned. One case study to which we apply these ideas is that of the Wiskott-Aldrich Syndrome Proteins as activators of actin polymerization. More generally, tethered ligands competing with those free in solution are common phenomena in biology, making this an important specific example of a widespread biological idea.

Additional Information

© 2009 Biophysical Society. Received 17 June 2008; accepted 31 October 2008. Editor: Arup Chakraborty. Available online 10 February 2009. We thank Lacramioara Bintu, John Dueber, Hernan Garcia, Paul Grayson, Alexander Grosberg, Jane Kondev, Wendell Lim, Tharathorn Rimchala, Boo Tseng, Paul Wiggins, and Brian Yeh for helpful discussions. D.V.V. and R.P. acknowledge the support of a Fannie and John Hertz Foundation Yaser Abu-Mustafa Fellowship, a University of California-Los Angeles/Caltech Medical Scientist Training Program Fellowship, and a National Institutes of Health Pioneer Award. M.H. acknowledges support from the National Science Foundation through NSF-DMR grant No. 0449184.

Additional details

Created:
August 20, 2023
Modified:
October 18, 2023