Issue 1, 2012

Dynamic optimization of signal transductionvia intrinsic disorder

Abstract

It is widely accepted that the inherent flexibility of intrinsically disordered proteins (IDPs) correlates with essential functions in the cell such as signaling. However, the mechanisms by which disorder dynamically facilitates and optimizes signal transduction remain unclear. In this study, we have used a computational protocol to evaluate the interplay between the intrinsic disorder of p27kip1 and the collective motions of its binding partners, cyclin dependent kinase 2 (CDK2) and cyclin A (CA). We found that the synergy between intrinsic disorder of p27kip1 and the essential collective motions of the CDK2–CA complex introduces a set of sequential steps to dynamically optimize signal transduction. Our observations indicate that optimized p27kip1-mediated signaling originates from a combination of adaptive folding, and the cooperativity between its residual disorder and the functional collective motions of the CDK2–CA complex.

Graphical abstract: Dynamic optimization of signal transductionvia intrinsic disorder

Supplementary files

Article information

Article type
Communication
Submitted
02 Oct 2011
Accepted
27 Oct 2011
First published
14 Nov 2011

Mol. BioSyst., 2012,8, 194-197

Dynamic optimization of signal transductionvia intrinsic disorder

L. M. Espinoza-Fonseca, Mol. BioSyst., 2012, 8, 194 DOI: 10.1039/C1MB05412K

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements