Amyloid precursor protein expression and accumulation of its intracellular fragment are required for exuberant neurite outgrowth associated with pathological presenilin 1 loss-of-function mutations before the emergence of amyloid burden in mice.
The conformational dynamics of multidrug resistance protein 1 (MRP1) are tracked in real time by single-molecule fluorescence resonance energy transfer experiments, which elucidate the rate-limiting mechanism of MRP1's transport cycle.
Oligomeric Amyloid-β and Tau, two proteins involved in Alzheimer's disease pathogenesis, require Amyloid Precursor Protein to enter neurons and exert their detrimental effect on synaptic plasticity and memory.
Reducing Akt-mediated huntingtin phosphorylation decreases APP accumulation at the synapse by reducing its anterograde axonal transport and ameliorates learning and memory in a mouse model of familial Alzheimer disease.
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.
In filamentous fungi the AP-2 complex, which in mammals is an adaptor of clathrin-mediated endocytosis, is recruited to specific clathrin-independent apical endocytosis necessary for proper lipid maintenance and polar growth.