双栖小泡蛋白和N-WASP调节肌蛋白组装的相互作用动力学

Amphiphysin 1, an endocytic adaptor concentrated at synapses
that couples clathrin-mediated endocytosis to dynamin-dependent
fission,wasalsoshownto have a regulatory role in actindynamics.
Here, we report that amphiphysin 1 interacts with N-WASP
and stimulates N-WASP- and Arp2/3-dependent actin polymerization.
Both the Src homology 3 and the N-BAR domains are
requiredforthisstimulation.Acidicliposome-triggered,N-WASPdependent
actin polymerization is strongly impaired in brain
cytosol of amphiphysin 1 knock-out mice. FRET-FLIM analysis of
Sertoli cells, where endogenously expressed amphiphysin 1 colocalizes
with N-WASP in peripheral ruffles, confirmed the
association between the two proteins in vivo. This association
undergoes regulation and is enhanced by stimulating phosphatidylserine
receptors on the cell surface with phosphatidylserine-
containing liposomes that trigger ruffle formation.
These results indicate that actin regulation is a key function of
amphiphysin 1 and that such function cooperates with the endocytic
adaptor role and membrane shaping/curvature sensing
properties of the protein during the endocytic reaction. 超快门宽增强型CCD相机