Highlights from The FEBS Journal - October 2017
The highlights from Issue 20 include a Discovery-in-Context Review on focal adhesions by Keith Burridge and the Editor's Choice article describing the binding mechanism between a WASP disordered region with the Cdc42 GTPase.
Focal adhesions: a personal perspective on a half century of progress
Keith Burridge (2017), The FEBS Journal, doi: 10.1111/febs.14195
Focal adhesions are sites of interaction between the actin cytoskeleton and the extracellular matrix mediated by clustered integrin receptors on the plasma membrane. In this Discovery-in-Context Review, Keith Burridge provides a personal account on the development of the field of focal adhesion research, beginning with the initial description of focal adhesions almost 50 years ago, to the identification of the structural components of focal adhesions and their role in many signalling pathways.
The dock-and-coalesce mechanism for the association of a WASP disordered region with the Cdc42 GTPase
Zhou and colleagues (2017), The FEBS Journal, doi: 10.1111/febs.14197
Intrinsically disordered proteins (IDPs) undergo folding upon binding to their interacting partners. Using the Wiskott-Aldrich Syndrome protein (WASP) and its binding partner, the Cdc42 GTPase, Zhou and colleagues show that binding begins with diffusion-dependent docking between the intrinsically disordered GTPase-binding domain (GBD) of WASP and its cognate binding site on Cdc42, and subsequently the remaining segments of WASP coalesce around their Cdc42 subsites. The authors also show that the rate of the docking step is the main contributor to the association rate constant of this two-step binding process.