摘要
A major player in membrane traffic, the large GTPase dynamin, is known in the actin dynamics field for its indirect association with the actin cytoskeleton via actin-binding proteins (ABPs) like cortactin. In this issue of The EMBO Journal, Gu et al extend this picture by revealing a direct interaction between dynamin and F-actin. They further show that oligomerized dynamin kicks off the gelsolin cap at the barbed ends of filaments. This study not only provides an interesting link between actin remodelling and membrane dynamics via dynamin, but also sheds light on the long-standing mystery of how barbed ends are liberated from the high-affinity capping protein gelsolin.
- 出版日期2010-11-3