CALM在指导VAMP2运输方面的证据。
Evidence for CALM in directing VAMP2 trafficking.
作者信息
Harel Asaff, Wu Fangbai, Mattson Mark P, Morris Christa M, Yao Pamela J
机构信息
Laboratory of Neurosciences, National Institute on Aging Intramural Research Program, Baltimore, MD 21224, USA.
出版信息
Traffic. 2008 Mar;9(3):417-29. doi: 10.1111/j.1600-0854.2007.00694.x. Epub 2007 Dec 21.
Clathrin assembly lymphoid myeloid leukemia protein (CALM) is a clathrin assembly protein with a domain structure similar to the neuron-specific assembly protein AP180. We have previously found that CALM is expressed in neurons and present in synapses. We now report that CALM has a neuron-related function: it facilitates the endocytosis of the synaptic vesicle protein VAMP2 from the plasma membrane. Overexpression of CALM leads to the reduction of cell surface VAMP2, whereas knockdown of CALM by RNA interference results in the accumulation of surface VAMP2. The AP180 N-terminal homology (ANTH) domain of CALM is required for its effect on VAMP2 trafficking, and the ANTH domain itself acts as a dominant-negative mutant. Thus, our results reveal a role for CALM in directing VAMP2 trafficking during endocytosis.
网格蛋白组装淋巴样髓样白血病蛋白（CALM）是一种网格蛋白组装蛋白，其结构域结构与神经元特异性组装蛋白AP180相似。我们之前发现CALM在神经元中表达并存在于突触中。我们现在报告CALM具有与神经元相关的功能：它促进突触囊泡蛋白VAMP2从质膜的内吞作用。CALM的过表达导致细胞表面VAMP2减少，而通过RNA干扰敲低CALM则导致表面VAMP2积累。CALM的AP180 N端同源（ANTH）结构域对其对VAMP2转运的作用是必需的，并且ANTH结构域本身作为显性负性突变体起作用。因此，我们的结果揭示了CALM在指导内吞作用期间VAMP2转运中的作用。
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