The 24 ANK repeats of each ankyrin are inhibited by combinatorial bindings of multiple disordered segments from their tail regions, suggesting a mechanism for differential regulations of membrane target bindings by ankyrins.

Biophysical and functional data strongly support the notion that Munc18-1 acts as a template to assemble the neuronal SNARE complex, and that inhibition of this activity underlies diverse forms of regulation of neurotransmitter release.

A catalytically dead paralog activates its cognate enzyme through an allosteric mechanism that combined structural and phylogenomic analysis indicates arose through acquisition of a dimerization domain, suggesting a general model for how complex allostery evolves.

PlexinD1 binding releases GIPC autoinhibition, leading to formation of high-order oligomers of the GIPC/myosin VI complex.

A key B-cell tyrosine kinase that adopts an autoinhibited conformation, and can be activated by either membrane recruitment or soluble inositol hexakisphosphates in solution.

In vitro reconstitution of the core focal adhesion proteins talin and vinculin with actin reveals lipid-dependent release of autoinhibition.

The Par complex controls spindle orientation during asymmetric cell division by phosphorylating the tumor suppressor Discs large, overcoming its autoinhibited state, and allowing it to bind the microtubule-binding protein GukHolder.

A key activator of Ras signaling adopts an autoinhibited, dimeric conformation that is activated by membrane and calcium binding.

A four-switch long-range allosteric network controls FGF receptor kinase conformational dynamics as well as activity and is applicable to other receptor tyrosine kinases.

The high-resolution X-ray crystal structure of PLC-γ1 reveals a unifying model for the regulation of the PLC-γ isozymes.