Biochemical and instrumental analysis showed that the membrane-induced exposure of myristoyl from the MA protein of Mason-Pfizer monkey virus triggers allosteric conformational changes resulting in MA oligomerization and unfolding of the cleavage site between MA and downstream domains of Gag.

The target-myristoyl switch induced by protein-protein interaction is a novel regulatory mechanism for myristoylated EF-hand calcium-binding proteins, in which target binding facilitates exposure of the myristoyl anchor and the association to the lipid membrane in a calcium-independent manner.

The cellular membrane competes with Abl for myristoyl binding to stabilize the preactivated state and enhance allosteric activation.

BART is a co-GEF for ARL3 and maintains the active ARL3-GTP until it is recycled by ARL3 effectors.

Unbiased molecular dynamics simulations reveal the insertion mechanism of the lipidated tail of the matrix domain of HIV-1 Gag into realistic membrane models and show its effect on lipid sorting.

A new structure reveals two Arf-GEF regulatory domains form a single structural unit that stimulates Arf-GEF activity.

Myristoylation of a secreted protein, identified in a global myristoylation analysis of the eukaryotic parasite Toxoplasma gondii, is important for host cell invasion.

PI(4,5)P2 plays a much broader role during the HIV-1 particle assembly process than assumed; it is indispensable not only for recruitment of Gag to the plasma membrane but also for the maintenance of Gag assemblies.

High-resolution NMR data and precise kinase activity assays on Abelson kinase bearing mutations in its αI-helix identify the αI-helix parts involved in disassembly of Abelson’s regulatory core and kinase activation.

The planar polarized organization of vestibular hair cells in the mouse inner ear is determined by the coordinated activities of the STK32A kinase and the transcription factor EMX2 to regulate the orphan receptor GPR156.