Suppr超能文献

CALM,网格蛋白组装蛋白,影响细胞表面 GluR2 的丰度。

CALM, a clathrin assembly protein, influences cell surface GluR2 abundance.

机构信息

Laboratory of Neurosciences, National Institute on Aging Intramural Research Program, NIH, 251 Bayview Boulevard, Baltimore, MD 21224, USA.

出版信息

Neuromolecular Med. 2011 Mar;13(1):88-90. doi: 10.1007/s12017-010-8142-6. Epub 2011 Jan 8.

Abstract

The clathrin assembly protein, CALM, promotes the assembly of clathrin-coated vesicles. In a previous study, we showed that CALM controls the level of the synaptic vesicle protein VAMP2 at the plasma membrane by regulating VAMP2 endocytosis. Here, we provide evidence that CALM also influences the cell surface level of the AMPA receptor subunit GluR2. Although mechanistic details as well as the physiological relevance of CALM and GluR2 in the neuron have yet to be established, CALM-mediated trafficking could function as a component of a dedicated system for controlling postsynaptic abundance of GluR2.

摘要

网格蛋白装配蛋白 CALM 促进网格蛋白包被囊泡的组装。在之前的研究中,我们发现 CALM 通过调节 VAMP2 内吞作用来控制质膜上突触囊泡蛋白 VAMP2 的水平。在这里,我们提供的证据表明,CALM 还会影响 AMPA 受体亚基 GluR2 的细胞表面水平。尽管 CALM 和 GluR2 在神经元中的作用机制细节以及生理相关性尚未确定,但 CALM 介导的运输可以作为控制 GluR2 突触后丰度的专用系统的组成部分。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验