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A novel nE-dlg/SAP102-associated protein, p51-nedasin, related to the amidohydrolase superfamily, interferes with the association between nE-dlg/SAP102 and n-methyl-d-aspartate receptor

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JOURnAL OF BIOLOGICAL CHEMISTRY 1999年第45期274卷 32204-32214页

作者： Kuwahara, H Araki, n Makino, K Masuko, n Honda, S Kaibuchi, K Fukunaga, K Miyamoto, E Ogawa, M Saya, H Kumamoto Univ Sch Med Dept Tumor Genet & Biol Kumamoto 8600811 Japan Kumamoto Univ Sch Med Dept Surg 2 Kumamoto 8600811 Japan Nara Inst Sci & Technol Div Signal Transduct Ikoma 6300101 Japan Kumamoto Univ Sch Med Dept Pharmacol Kumamoto 8600811 Japan

The membrane-associated guanylate kinase proteins have been known to interact various membrane receptors with their n-terminal segments designated the PdZ domains and to cluster these receptors at the target site of the cell membrane. nE-dlg/SAP102, a neuronal and endocrine tissue-specific MAGUK family protein, was found to be expressed in both dendrites and cell bodies in neuronal cells. Although nE-dlg/SAP102 localized at dendrites was shown to interact with n-methyl-d-aspartate receptor 2B via the PdZ domains to compose postsynaptic density, the binding proteins existing in the cell body of the neuron are still unknown. Here we report the isolation of a novel nE-dlg/SAP102-associated protein, p51-nedasin. nedasin has a significant homology with amidohydrolase superfamily proteins and shows identical sequences to a recently identified protein that has guanine aminohydrolase activity. nedasin has four alternative splice variants (S, Vf, V2, and V3) that exhibited different C-terminal structures. nE-dlg/SAP102 is shown to interact with only the S form of nedasin which is predominantly expressed in brain. The expression of nedasin in neuronal cells increases in parallel with the progress of synaptogenesis and is mainly detected in cell bodies where it co-localizes with nE-dlg/SAP102, Furthermore, nedasin interferes with the association between nE-dlg/SAP102 and nMdA receptor 2B in vitro. These findings suggest that alternative splicing of nedasin may play a role in the formation and/or structural change in synapses during neuronal development by modifying clustering of neurotransmitter receptors at the synaptic sites.

关键词：衔接蛋白质类信号转导选择性剪接酰胺基水解酶类/代谢氨基酸序列氨基水解酶类/遗传学氨基水解酶类/代谢碱基序列细胞培养的染色体显带基因肿瘤抑制膜蛋白质类分子序列数据神经元/化学神经肽类/代谢核蛋白质类蛋白质类/代谢受体 n-甲基-d-天冬氨酸/代谢序列比对表面等离激元转录因子动物牛大鼠

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Kinesin superfamily motor protein KIF17 and mLin-10 in nMdA receptor - Containing vesicle transport

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SCIEnCE 2000年第5472期288卷 1796-1802页

作者： Setou, M nakagawa, T Seog, dH Hirokawa, n Univ Tokyo Grad Sch Med Dept Cell Biol & Anat Bunkyo Ku Tokyo Japan

Experiments with vesicles containing n-methyl-d-aspartate (nMdA) receptor 2B (nR2B subunit) show that they are transported along microtubules by KIF17, a neuron-specific molecular motor in neuronal dendrites. Selective transport is accomplished by direct interaction of the KIF17 tail with a PdZ domain of mLin-10 (Mintl1/X11), which is a constituent of a large protein complex including mLin-2 (CASK), mLin-7 (MALS/VeLis), and the nR2B subunit. This interaction, specific for a neurotransmitter receptor critically important for plasticity in the postsynaptic terminal, may be a regulatory point for synaptic plasticity and neuronal morphogenesis.

关键词：氨基酸特征结构氨基酸序列结合部位生物转运漂亮新小杆线虫蛋白质类克隆分子树突/代谢二聚作用驱动蛋白/化学驱动蛋白/遗传学驱动蛋白/代谢膜蛋白质类微管/代谢模型生物学分子马达蛋白质类/化学分子马达蛋白质类/遗传学分子马达蛋白质类/代谢分子序列数据分子量细胞器/代谢沉淀素试验蛋白质结合蛋白质类/化学蛋白质类/代谢受体 n-甲基-d-天冬氨酸/代谢重组蛋白质类/化学重组蛋白质类/代谢双杂交系统技术动物男(雄)性小鼠

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Three isoforms of synaptic scaffolding molecule and their characterization -: Multimerization between the isoforms and their interaction with n-methyl-d-aspartate receptors and SAP90/PSd-95-associated protein

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JOURnAL OF BIOLOGICAL CHEMISTRY 2000年第4期275卷 2966-2972页

作者： Hirao, K Hata, Y Yao, I deguchi, M Kawabe, H Mizoguchi, A Takai, Y JCR Pharmaceut Co Ltd Japan Sci & Technol Corp ERATO Takai Biotimer ProjectNishi Ku Kobe Hyogo 6512241 Japan Tokyo Med & Dent Univ Dept Med Biochem Bunkyo Ku Tokyo 1138519 Japan Osaka Univ Grad Sch Med Fac Med Dept Mol Biol & Biochem Suita Osaka 5650871 Japan Kyoto Univ Grad Sch Dept Anat & Neurobiol Kyoto 6068315 Japan

The synaptic scaffolding molecule (S-SCAM) has been identified as a protein interacting with SAP90/PSd-95-associated protein (SAPAP) (also called guanylate kinase-associated protein/hdLG-associated protein). S-SCAM;I has six PdZ (we have numbered them PdZ-0 to -5), two WV, and one guanylate kinase (GK) domains and interacts with n-methyl-d-aspartate (nMdA) receptor via PdZ-5 and SAPAP via the GIC domain. me have identified here shorter isoforms of S-SCAM that start at the 164th or 224th methionine, and we renamed the original one, S-SCAM alpha, the middle one, S-SCAM beta, and the shortest one, SSCAM-gamma. S-SCAM beta and -gamma have five PdZ (PdZ-1 to -5), two WW, and one GK domains. S-SCAM alpha interacted with S-SCAM beta and -gamma through the region containing PdZ-4 and -5. The region containing both of PdZ-4 and -5 is sufficient for the clustering of nMdA receptors and forms a dimer in gel filtration, suggesting that S-SCAM forms multimers via the interaction between the C-terminal PdZ domains and assembles nMdA receptors into clusters. S-SCAM beta P and -gamma also interacted with SAPAP, suggesting that the n-terminal region of the GH domain is not necessary for the interaction. Finally, we have identified the interaction of the PdZ domains of S-SCAM with the GK domain of PSd-95/SAP90. S-SCAM PSd-95/SAP90, and SAPAP are colocalized at least in some part in brain. Therefore, S-SCAM, PSd-95/SAP90, and SA-PAP may form a complex in vivo.

关键词：衔接蛋白质类信号转导氨基酸序列碱基序列生物聚合物 CHO细胞 COS细胞载体蛋白质类/化学载体蛋白质类/代谢小脑/代谢色谱法凝胶仓鼠亚科 dnA引物显微镜检查荧光分子序列数据神经组织蛋白质类/化学神经组织蛋白质类/代谢蛋白质结合蛋白质亚型/化学蛋白质亚型/代谢受体 n-甲基-d-天冬氨酸/代谢视网膜/代谢序列同源性氨基酸动物大鼠

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Interaction of the n-methyl-d-aspartic acid receptor nR2d subunit with the c-Abl tyrosine kinase

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JOURnAL OF BIOLOGICAL CHEMISTRY 2000年第17期275卷 12725-12729页

作者： Glover, RT Angiolieri, M Kelly, S Monaghan, dT Wang, JYJ Smithgall, TE Buller, AL Univ Pittsburgh Dept Neurosci Pittsburgh PA 15260 USA Univ Nebraska Dept Biol Omaha NE 68154 USA Univ Pittsburgh Sch Med Dept Mol Genet & Biochem Pittsburgh PA 15261 USA Univ Nebraska Med Ctr Dept Pharmacol Omaha NE 68198 USA Univ Calif San Diego Dept Biol La Jolla CA 92093 USA

The COOH-terminal domain of the nR2d subunit of the nMdA receptor contains proline-rich regions that show striking homology to sequences known to bind to Src homology 3 (SH3) domains. To determine whether the proline-rich region of the nR2d subunit interacts with specific SH3 domains, in vitro SH3 domain binding assays were performed. A proline-rich fragment of the nR2d subunit (2d(866-1064)) bound to the Abl SH3 domain but not to the SH3 domains from Src, Fyn, Grb2, GAP, or phospholipase C-gamma (PLC gamma). Co-immunoprecipitation of nR2d with Abl suggests stable association of nR2d and Abl in transfected cells. The SH3 domain plays an important role in the negative regulation of Abl kinase activity. To determine whether the interaction of nR2d with the Abl SH3 domain alters Abl kinase activity, Abl was expressed alone or with nR2d in 293T cells. Autophosphorylation of Abl was readily observed when Abl was expressed alone. However, co-expression of Abl with 2d(866-1064) or full-length nR2d inhibited autophosphorylation. 2d(866-1064) did not inhibit delta SH3 Abl, indicating a requirement for the Abl SH3 domain in the inhibitory effect, Similarly, 2d(866-1064) did not inhibit the catalytic activity of Abl-PP, which contains two point mutations in the SH2-kinase linker domain that release the negative kinase regulation by the SH3 domain. In contrast, the full-length nR2d subunit partially inhibited the autokinase activity of both delta SH3 Abl and Abl-PP, suggesting that nR2d and Abl may interact at multiple sites. Taken together, the data in this report provide the first evidence for a novel inhibitory interaction between the nR2d subunit of the MMdA receptor and the Abl tyrosine kinase.

关键词：氨基酸序列细胞系克隆分子表位大肠杆菌/代谢免疫印迹法分子序列数据诱变定点沉淀素试验原癌基因蛋白质c-abl/代谢受体 n-甲基-d-天冬氨酸/化学受体 n-甲基-d-天冬氨酸/代谢重组融合蛋白质类/代谢 src同源域人类

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Shank, a novel family of postsynaptic density proteins that binds to the nMdA receptor/PSd-95/GKAP complex and cortactin

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nEUROn 1999年第3期23卷 569-582页

作者： naisbitt, S Kim, E Tu, JC Xiao, B Sala, C Valtschanoff, J Weinberg, RJ Worley, PF Sheng, M Massachusetts Gen Hosp Dept Neurobiol Howard Hughes Med Inst Boston MA 02114 USA Harvard Med Sch Boston MA 02114 USA Johns Hopkins Univ Sch Med Dept Neurosci Baltimore MD 21205 USA Univ N Carolina Dept Cell Biol & Anat Chapel Hill NC 27599 USA Pusan Natl Univ Dept Pharmacol Pusan 609735 South Korea

nMdA receptors are linked to intracellular cytoskeletal and signaling molecules via the PSd-95 protein complex. We report a novel family of postsynaptic density (PSd) proteins, termed Shank, that binds via its PdZ domain to the C terminus of PSd-95-associated protein GKAP. A ternary complex of Shank/GKAP/PSd-95 assembles in heterologous cells and can be coimmunoprecipitated from rat brain. Synaptic localization of Shank in neurons is inhibited by a GKAP splice variant that lacks the Shank-binding C terminus. In addition to its PdZ domain, Shank contains a proline-rich region that binds to cortactin and a SAM domain that mediates multimerization. Shank may function as a scaffold protein in the PSd, potentially cross-linking nMdA receptor/PSd-95 complexes and coupling them to regulators of the actin cytoskeleton.

关键词：肌动蛋白类/代谢衔接蛋白质类信号转导 COS细胞载体蛋白质类/分析载体蛋白质类/化学载体蛋白质类/遗传学载体蛋白质类/代谢皮动蛋白细胞骨架/化学细胞骨架/超微结构海马/细胞学细胞内信号肽和蛋白质类膜蛋白质类微丝蛋白质类/分析微丝蛋白质类/代谢显微镜检查免疫电子分子序列数据多基因族神经组织蛋白质类/分析神经组织蛋白质类/代谢神经元/化学神经元/细胞学神经元/代谢蛋白质结构三级受体 n-甲基-d-天冬氨酸/分析受体 n-甲基-d-天冬氨酸/代谢序列同源性氨基酸突触/化学突触/代谢突触/超微结构动物兔大鼠

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Glutamate receptors regulate actin-based plasticity in dendritic spines

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nATURE nEUROSCIEnCE 2000年第9期3卷 887-894页

作者： Fischer, M Kaech, S Wagner, U Brinkhaus, H Matus, A Friedrich Miescher Inst CH-4002 Basel Switzerland

dendritic spines at excitatory synapses undergo rapid, actin-dependent shape changes which may contribute to plasticity in brain circuits. Here we show that actin dynamics in spines are potently inhibited by activation of either AMPA or nMdA subtype glutamate receptors. Activation of either receptor type inhibited actin-based protrusive activity from the spine head. This blockade of motility caused spines to round up so that spine morphology became both more stable and more regular. Inhibition of spine motility by AMPA receptors was dependent on postsynaptic membrane depolarization and influx of Ca2+ through voltage-activated channels. In combination with previous studies, our results suggest a two-step process in which spines initially formed in response to nMdA receptor activation are subsequently stabilized by AMPA receptors.

关键词：肌动蛋白类/代谢钙/代谢细胞运动/药物作用细胞运动/生理学细胞大小/药物作用细胞大小/生理学细胞培养的树突/药物作用树突/代谢树突/超微结构绿色荧光蛋白质类海马/药物作用海马/代谢海马/超微结构发光蛋白质类/遗传学膜电位/药物作用膜电位/生理学小鼠转基因神经元可塑性/药物作用神经元可塑性/生理学器官培养技术受体 AMPA/药物作用受体 AMPA/代谢受体谷氨酸/药物作用受体谷氨酸/代谢受体 n-甲基-d-天冬氨酸/药物作用受体 n-甲基-d-天冬氨酸/代谢突触/药物作用突触/代谢突触/超微结构动物小鼠

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Kainate receptors are involved in synaptic plasticity

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nATURE 1999年第6759期402卷 297-301页

作者： Bortolotto, ZA Clarke, VRJ delany, CM Parry, MC Smolders, I Vignes, M Ho, KH Miu, P Brinton, BT Fantaske, R Ogden, A Gates, M Ornstein, PL Lodge, d Bleakman, d Collingridge, GL Univ Bristol Sch Med Dept Anat MRC Ctr Synapt Plast Bristol BS8 1TD Avon England Free Univ Brussels Inst Pharmaceut Dept Pharmaceut Chem & Drug Anal B-1090 Brussels Belgium Univ Montpellier 2 Lab Plasticite Cerebrale CNRS F-34095 Montpellier France Allelix Biopharmaceut Mississauga ON L4V 1V7 Canada Eli Lilly & Co Lilly Corp Ctr Indianapolis IN 46285 USA

The ability of synapses to modify their synaptic strength in response to activity is a fundamental property of the nervous system and may be an essential component of learning and memory(1). There are three classes of ionotropic glutamate receptor, namely nMdA (n-methyl-d-aspartate), AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole-4-propionic acid) and kainate receptors(2);critical roles in synaptic plasticity have been identified for two of these. Thus, at many synapses in the brain, transient activation of nMdA receptors leads to a persistent modification in the strength of synaptic transmission mediated by AMPA receptors(3,4). Here, to determine whether kainate receptors(5-7) are involved in synaptic plasticity, we have used a new antagonist, LY382884 ((3S, 4aR, 6S, 8aR)-6-( (4-carboxyphenyl)methyl-1,2,3,4,4a,5,6,7,8,8a-decahydroisoquinoline-3-carboxylic acid), which antagonizes kainate receptors at concentrations that do not affect AMPA or nMdA receptors. We find that LY382884 is a selective antagonist at neuronal kainate receptors containing the GluR5 subunit. it has no effect on long-term potentiation (LTP) that is dependent on nMdA receptors but prevents the induction of mossy fibre LTP, which is independent of nMdA receptors. Thus, kainate receptors can act as the induction trigger for longterm changes in synaptic transmission.

关键词：细胞系兴奋性氨基酸拮抗剂/药理学兴奋性突触后电位海马/生理学异喹啉类/药理学犬尿烯酸/药理学长时程增强/药物作用长时程增强/生理学苔藓纤维海马/生理学大鼠 Sprague-dawley 受体 AMPA/药物作用受体 AMPA/代谢受体红藻氨酸/拮抗剂和抑制剂受体红藻氨酸/生理学受体 n-甲基-d-天冬氨酸/药物作用受体 n-甲基-d-天冬氨酸/代谢突触/生理学突触膜/代谢突触传递动物人类大鼠

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different modes of expression of AMPA and nMdA receptors in hippocampal synapses

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nATURE nEUROSCIEnCE 1999年第7期2卷 618-624页

作者： Takumi, Y Ramírez-León, V Laake, P Rinvik, E Ottersen, OP Univ Oslo Inst Basic Med Sci Dept Anat N-0317 Oslo Norway Hirosaki Univ Sch Med Dept Otorhinolaryngol Hirosaki Aomori 0368562 Japan Karolinska Inst Dept Neurosci S-17177 Stockholm Sweden Univ Oslo Sect Med Stat N-0317 Oslo Norway

Postembedding immunogold labeling was used to determine the relationship between AMPA and nMdA receptor density and size of Schaffer collateral-commissural (SCC) synapses of the adult rat. All SCC synapses expressed nMdA receptors. AMPA and nMdA receptors were colocalized in at least 75% of SCC synapses;the ratio of AMPA to nMdA receptors was a linear function of postsynaptic density (PSd) diameter, with AMPA receptor number dropping to zero at a PSd diameter of similar to 180 nm. These findings indicate that 'silent' SCC synapses are smaller than the majority of SCC synapses at which AMPA and nMdA receptors are colocalized. Thus synapse size may determine important properties of SCC synapses.

关键词：海马/代谢海马/超微结构显微镜检查免疫电子大鼠 Wistar 受体 AMPA/分析受体 AMPA/代谢受体 n-甲基-d-天冬氨酸/分析受体 n-甲基-d-天冬氨酸/代谢回归分析突触/代谢突触/超微结构动物男(雄)性大鼠

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Zn²⁺:: A novel ionic mediator of neural injury in brain disease (vol 21, pg 395, 2000)

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TREndS In PHARMACOLOGICAL SCIEnCES 2000年第12期21卷 496-496页

作者： Weiss, JH Sensi, SL Koh, JY UniversityofCalifornia IrvineCA92697-4292USA.jweiss@uci.edu

Zn2+ is the second most prevalent trace element in the body and is present in particularly large concentrations in the mammalian brain. Although Zn^2+ is a cofactor for many enzymes in all tissues, a unique feature of brain Zn^2+ is its vesicular localization in presynaptic terminals, where its release is dependent on neural activity. Although the physiological significance of synaptic Zn^2+ release is little understood, it probably plays a modulatory role in synaptic transmission. Furthermore, several lines of evidence support the idea that, upon excessive synaptic Zn^2+ release, its accumulation in postsynaptic neurons contributes to the selective neuronal loss that is associated with certain acute conditions, including epilepsy and transient global ischaemia. More speculatively, Zn^2+ dis-homeostasis might also contribute to some degenerative conditions, including Alzheimer's disease. Further elucidation of the pathological actions of Zn^2+ in the brain should result in new therapeutic approaches to these conditions.

关键词：脑疾病/代谢钙通道/代谢神经变性疾病/病因学神经变性疾病/代谢神经元/代谢突触前末梢/代谢受体 n-甲基-d-天冬氨酸/代谢信号传导/生理学锌/代谢锌/生理学动物人类

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SAP family proteins

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BIOCHEMICAL And BIOPHYSICAL RESEARCH COMMUnICATIOnS 2000年第1期269卷 1-6页

作者： Fujita, A Kurachi, Y Osaka Univ Grad Sch Med Dept Pharmacol 2 Osaka 5650871 Japan

Thus far, five members including dlg, SAP97/hdlg, SAP90/PSd-95, SAP102, and PSd-93/chapsyn110 which belong to SAP family have been identified. Recent studies have revealed that these proteins play important roles in the localization and function of glutamate receptors and K+ channels. Although most of them have been reported to be localized to the synapse, only one member, SAP97, is expressed also in the epithelial cells. In this review, we have summarized structural characters of SAP family proteins and discuss their functions in neurons and epithelial cells. (C) 2000 Academic Press.

关键词：衔接蛋白质类信号转导氨基酸特征结构上皮细胞/代谢膜蛋白质类神经组织蛋白质类/化学神经组织蛋白质类/代谢钾通道/代谢受体谷氨酸/代谢受体红藻氨酸/代谢受体 n-甲基-d-天冬氨酸/代谢突触/代谢动物人类

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