Hinshaw J E
Laboratory of Cell Biochemistry and Biology, National Institutes of Health, Bethesda, Maryland 20892, USA.
Annu Rev Cell Dev Biol. 2000;16:483-519. doi: 10.1146/annurev.cellbio.16.1.483.
Dynamin, a 100-kDa GTPase, is an essential component of vesicle formation in receptor-mediated endocytosis, synaptic vesicle recycling, caveolae internalization, and possibly vesicle trafficking in and out of the Golgi. In addition to the GTPase domain, dynamin also contains a pleckstrin homology domain (PH) implicated in membrane binding, a GTPase effector domain (GED) shown to be essential for self-assembly and stimulated GTPase activity, and a C-terminal proline-rich domain (PRD), which contains several SH3-binding sites. Dynamin partners bind to the PRD and may either stimulate dynamin's GTPase activity or target dynamin to the plasma membrane. Purified dynamin readily self-assembles into rings or spirals. This striking structural property supports the hypothesis that dynamin wraps around the necks of budding vesicles where it plays a key role in membrane fission. The focus of this review is on the relationship between the GTPase and self-assembly properties of dynamin and its cellular function.
发动蛋白是一种100 kDa的GTP酶，是受体介导的内吞作用、突触小泡循环、小窝内吞作用以及可能进出高尔基体的小泡运输中囊泡形成的重要组成部分。除了GTP酶结构域，发动蛋白还包含一个与膜结合有关的普列克底物蛋白同源结构域（PH）、一个对自组装和受刺激的GTP酶活性至关重要的GTP酶效应结构域（GED）以及一个C端富含脯氨酸的结构域（PRD），该结构域包含几个SH3结合位点。发动蛋白结合蛋白与PRD结合，可能会刺激发动蛋白的GTP酶活性或将发动蛋白靶向质膜。纯化的发动蛋白很容易自组装成环或螺旋。这种显著的结构特性支持了这样一种假说，即发动蛋白缠绕在出芽囊泡的颈部，在膜裂变中起关键作用。本综述的重点是发动蛋白的GTP酶和自组装特性与其细胞功能之间的关系。
