Plexin controls the spatial distribution of synapses by locally inhibiting Rap2 small GTPase activity along the axon, and a Rap2 effector, TNIK, which also plays a key role in inhibiting synapse number.
Structure, dynamics, and mutation of a gamete fusion protein and comparisons to viral homologues suggest that after trimerization the domain bearing the membrane-inserting fusion loops can pivot with respect to the trimer 3-fold axis.
Cryo-EM reveals how a protein called NECAP inactivates the AP2 clathrin adaptor complex through concerted engagement of two domains which confer specificity for membrane-activated and phosphorylated AP2.
Small molecule antivirals that drive assembly of HBV capsid protein can also bind to pre-assembled capsids causing them to change morphology or even break, suggesting a complex transduction of binding effects across the capsid.
The sharp expression pattern driven by a classic, simple animal enhancer is determined by multiple molecular mechanisms, not only cooperative binding of the activating transcription factor as was previously thought.