Novel clusterin of sodium channel NaV1.1 with ankyrin-G and neurofascin at discrete sites in the inner plexiform layer of the retina

被引:36
作者
Van Wart, A
Boiko, T
Trimmer, JS
Matthews, G [1 ]
机构
[1] SUNY Stony Brook, Ctr Mol Med, Dept Neurobiol & Behav, Stony Brook, NY 11794 USA
[2] Univ Calif Davis, Sch Med, Dept Pharmacol, Davis, CA 95616 USA
关键词
D O I
10.1016/j.mcn.2004.11.012
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Voltage-gated sodium channels cluster at sites of action potential generation and propagation by interacting with partner proteins such as neurofascin, an adhesion molecule in the L1 family, and ankyrin-G, a spectrin-binding protein required for sodium channel accumulation at axon initial segments. Here, we describe in the inner plexiform layer of the retina a novel site of high-density sodium channel clustering, marked by ankyrin-G and neurofascin. The sodium channel isoform at this site is Na(v)1.1 instead of the Na(v)1.6 channels more commonly found in association with the clustering machinery. During development, Na(v)1.2 channels first associate with ankyrin-G in the inner plexiform layer but are later replaced by Na(v)1.1, similar to the switch from Na(v)1.2 to Na(v)1.6 at nodes of Ranvier and initial segments. This represents the first instance of high-density clustering of Na(v)1.1 channels, which may contribute to synaptic interactions among retinal neurons in the inner plexiform layer. (c) 2004 Elsevier Inc. All rights reserved.
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收藏
页码:661 / 673
页数:13
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