Dynamics of Auxilin 1 and GAK in clathrin-mediated traffic
Dynamics of Auxilin 1 and GAK in clathrin-mediated traffic
复制标题
网格蛋白介导的交通中辅助蛋白 1 和 GAK 的动态。
DOI:
10.1083/jcb.201908142
复制
发表时间:
2020-03-02
影响因子:
7.8
通讯作者:
Kirchhausen, Tom
中科院分区:
文献类型:
--
作者:
He, Kangmin;Song, Eli;Kirchhausen, Tom
Clathrin-coated vesicles lose their clathrin lattice within seconds of pinching off, through the action of the Hsc70 "uncoating ATPase." The J- and PTEN-like domain-containing proteins, auxilin 1 (Aux1) and auxilin 2 (GAK), recruit Hsc70. The PTEN-like domain has no phosphatase activity, but it can recognize phosphatidylinositol phosphate head groups. Aux1 and GAK appear on coated vesicles in successive transient bursts, immediately after dynamin-mediated membrane scission has released the vesicle from the plasma membrane. These bursts contain a very small number of auxilins, and even four to six molecules are sufficient to mediate uncoating. In contrast, we could not detect auxilins in abortive pits or at any time during coated pit assembly. We previously showed that clathrin-coated vesicles have a dynamic phosphoinositide landscape, and we have proposed that lipid head group recognition might determine the timing of Aux1 and GAK appearance. The differential recruitment of Aux1 and GAK correlates with temporal variations in phosphoinositide composition, consistent with a lipid-switch timing mechanism.