SynCAM1 通过蛋白 4.1B 招募 NMDA 受体。
SynCAM1 recruits NMDA receptors via protein 4.1B.
机构信息
Institute of Neuroscience, University of Oregon, Eugene, OR 97403, USA.
出版信息
Mol Cell Neurosci. 2009 Dec;42(4):466-83. doi: 10.1016/j.mcn.2009.09.010. Epub 2009 Sep 29.
Cell adhesion molecules have been implicated as key organizers of synaptic structures, but there is still a need to determine how these molecules facilitate neurotransmitter receptor recruitment to developing synapses. Here, we identify erythrocyte protein band 4.1-like 3 (protein 4.1B) as an intracellular effector molecule of Synaptic Cell Adhesion Molecule 1 (SynCAM1) that is sufficient to recruit NMDA-type receptors (NMDARs) to SynCAM1 adhesion sites in COS7 cells. Protein 4.1B in conjunction with SynCAM1 also increased the frequency of NMDAR-mediated mEPSCs and area of presynaptic contact in an HEK293 cell/ neuron co-culture assay. Studies in cultured hippocampal neurons reveal that manipulation of protein 4.1B expression levels specifically affects NMDAR-mediated activity and localization. Finally, further experimentation in COS7 cells show that SynCAM1 may also interact with protein 4.1N to specifically effect AMPA type receptor (AMPAR) recruitment. Thus, SynCAM1 may recruit both AMPARs and NMDARs by independent mechanisms during synapse formation.
细胞黏附分子被认为是突触结构的关键组织者，但仍需要确定这些分子如何促进神经递质受体募集到发育中的突触。在这里，我们确定红细胞蛋白带 4.1 样 3（蛋白 4.1B）作为突触细胞黏附分子 1（SynCAM1）的细胞内效应分子，足以将 NMDA 型受体（NMDAR）募集到 COS7 细胞中的 SynCAM1 黏附位点。蛋白 4.1B 与 SynCAM1 一起还增加了在 HEK293 细胞/神经元共培养测定中 NMDAR 介导的 mEPSC 的频率和突触前接触面积。在培养的海马神经元中的研究表明，蛋白 4.1B 表达水平的操纵特异性地影响 NMDAR 介导的活性和定位。最后，在 COS7 细胞中的进一步实验表明，SynCAM1 也可能与蛋白 4.1N 相互作用，以特异性地影响 AMPA 型受体（AMPAR）的募集。因此，SynCAM1 可能在突触形成过程中通过独立的机制募集 AMPAR 和 NMDAR。
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