A three amino acid tail following the TM4 region of the N-methyl-D-aspartate receptor (NR) 2 subunits is sufficient to overcome endoplasmic reticulum retention of NR1-1a subunit

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	A three amino acid tail following the TM4 region of the N-methyl-D-aspartate receptor (NR) 2 subunits is sufficient to overcome endoplasmic reticulum retention of NR1-1a subunit
	Yang, Wei ; Zheng, Chanying ; Song, Qilin ; Yang, Xiujuan ; Qiu, Shuang ; Liu, Chunqing ; Chen, Zhong ; Duan, Shumin ; Luo, Jianhong
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2007
卷号	282 期号:12 页码:9269-9278
关键词	C-TERMINAL DOMAIN CELL-SURFACE EXPRESSION NMDA RECEPTOR ER RETENTION CHANNEL TRAFFICKING GLUTAMATE SIGNAL PREASSOCIATION STOICHIOMETRY
ISSN号	0021-9258
通讯作者	Luo, JH (reprint author), Zhejiang Univ, Sch Med, Inst Neurosci, Dept Neurobiol, Hangzhou 3100058, Peoples R China,luojianhong@zju.edu.cn
英文摘要	The cytoplasmic C-terminal domains of NR2 subunits have been proposed to modulate the assembly and trafficking of NMDA receptors. However, questions remain concerning which domains in the C terminus of NR2 subunits control the assembly of receptor complexes and how the assembled complexes are selectively trafficked through the various cellular compartments such as endoplasmic reticulum (ER) to the cell surface. In the present study, we found that the three amino acid tail after the TM4 region of NR2 subunits is necessary for surface expression of functional NMDA receptors, while truncations with only two amino acids following the TM4 region (NR2 Delta 2) completely eliminated surface expression of the NMDA receptor on co-expression with NR1-1a in HEK293 cells. FRET (fluorescence resonance energy transfer) analysis showed that these NR2 Delta 2 truncations are able to form homomers and heteromers on co-expression with NR1-1a. Furthermore, when NR2 Delta 2 subunits were cotransfected with either the NR1-4a or NR1-1a(AAA) mutant, lacking the ER retention motif (RRR), functional NMDA receptors were detected in the transfected HEK293 cells. Unexpectedly, we found that the replacement of five residues after TM4 with alanines gave results indistinguishable from those of NR2B Delta 5 (EHLFY), demonstrating the short tail following the TM4 of NR2 subunits is not sequence-specific-dependent. Taken together, our results show that the C terminus of the NR2 subunits is not necessary for the assembly of NMDA receptor complexes, whereas a three amino acid long cytoplasmic tail following the TM4 of NR2 subunits is sufficient to overcome the ER retention existing in the C terminus of NR1, allowing the assembled NMDA receptors to reach the cell surface.
学科主题	Biochemistry & Molecular Biology
收录类别	SCI
语种	英语
公开日期	2012-07-23
内容类型	期刊论文
源URL	[http://ir.sibs.ac.cn/handle/331001/1781]
专题	上海神经科学研究所_神经所(总)
推荐引用方式 GB/T 7714	Yang, Wei,Zheng, Chanying,Song, Qilin,et al. A three amino acid tail following the TM4 region of the N-methyl-D-aspartate receptor (NR) 2 subunits is sufficient to overcome endoplasmic reticulum retention of NR1-1a subunit[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2007,282(12):9269-9278.
APA	Yang, Wei.,Zheng, Chanying.,Song, Qilin.,Yang, Xiujuan.,Qiu, Shuang.,...&Luo, Jianhong.(2007).A three amino acid tail following the TM4 region of the N-methyl-D-aspartate receptor (NR) 2 subunits is sufficient to overcome endoplasmic reticulum retention of NR1-1a subunit.JOURNAL OF BIOLOGICAL CHEMISTRY,282(12),9269-9278.
MLA	Yang, Wei,et al."A three amino acid tail following the TM4 region of the N-methyl-D-aspartate receptor (NR) 2 subunits is sufficient to overcome endoplasmic reticulum retention of NR1-1a subunit".JOURNAL OF BIOLOGICAL CHEMISTRY 282.12(2007):9269-9278.