Tamalin-KO 基因敲除小鼠

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产品名称

Tamalin-KO 基因敲除小鼠

产品编号

S-KO-10716

品系全称

C57BL/6JCya-Tamalinem1/Cya

品系背景

C57BL/6JCya

品系编号

KOCMP-56149-Tamalin-B6J-VA

品系状态

使用本品系发表的文献需注明: Tamalin-KO 基因敲除小鼠 mice (Strain S-KO-10716) were purchased from Cyagen.
交付类型
周龄
性别
基因型
数量

基本信息

基因研究概述

质控标准

基因
基因全称
trafficking regulator and scaffold protein tamalin
基因别称
Grasp
染色体号
Chr 15 (Mouse)
转录本 ID
NCBI: NM_019518.3 | Ensembl: ENSMUST00000000543
修饰方式
全身性基因敲除
靶向范围
Exon 1~8
敲除长度
~7712 bp
品系说明
该品系是基于策略设计时的数据库信息制作而成,建议您在购买前查询最新的数据库和相关文献,以获取最准确的表型信息。
表型提示
MGI:1860303Mice homozygous for targeted null mutations develop and behave normally under ordinary conditions but display a marked reduction in sensitivity to acute morphine responses and impaired adaptive responses to morphine and cocaine.
Tamalin,也称为GRASP-1(Golgi reassembly stacking protein 1),是一种在神经元中发挥重要功能的蛋白质。Tamalin是一种支架蛋白,参与调控膜转运、细胞骨架动力学以及信号转导等多种细胞过程。Tamalin通过其PDZ结构域与多种蛋白质相互作用,包括cytohesin-2/ARNO、ARF1、ARF6、EFA6A、Dock180、HCN2、S-SCAM和Mint2等,从而影响这些蛋白质的功能和定位。

Tamalin在神经系统发育和功能中发挥重要作用。研究发现,Tamalin缺失会导致小鼠海马神经元中的树突生长和分支减少,同时也会降低电惊厥休克(ECS)诱导的成年小鼠海马神经发生和树突分支[1,2]。此外,Tamalin还与神经母细胞瘤的发生和发展有关,其表达上调与不良预后相关[4]。

Tamalin还参与调控多种信号通路,包括mGluR5信号通路和HCN通道信号通路。研究发现,Tamalin是mGluR5的一个支架蛋白,通过调节mGluR5的定位和内吞作用,影响mGluR5信号转导[3,7]。此外,Tamalin还与HCN2通道相互作用,形成蛋白质复合物,调节HCN2通道的功能和定位[6]。

Tamalin的表达和功能也受到多种因素的调控。例如,研究发现,IFN-β可以上调截断的TrkC受体TrkC-T1的表达,抑制NT3的信号转导和抗凋亡活性,而Tamalin在IFN-β介导的NT3信号抑制中发挥重要作用[5]。

Tamalin的研究有助于深入理解神经元发育和功能调控的分子机制,为神经系统疾病的治疗和预防提供新的思路和策略。

参考文献:
1. Yanpallewar, Sudhirkumar U, Barrick, Colleen A, Palko, Mary Ellen, Fulgenzi, Gianluca, Tessarollo, Lino. . Tamalin is a critical mediator of electroconvulsive shock-induced adult neuroplasticity. In The Journal of neuroscience : the official journal of the Society for Neuroscience, 32, 2252-62. doi:10.1523/JNEUROSCI.5493-11.2012. https://pubmed.ncbi.nlm.nih.gov/22396401/
2. Mo, Jiwon, Choi, Sukwoo, Ahn, Poong Gi, Lee, Hyun Woo, Kim, Hyun. 2012. PDZ-scaffold protein, Tamalin promotes dendritic outgrowth and arborization in rat hippocampal neuron. In Biochemical and biophysical research communications, 422, 250-5. doi:10.1016/j.bbrc.2012.04.136. https://pubmed.ncbi.nlm.nih.gov/22569042/
3. Matosin, Natalie, Fernandez-Enright, Francesca, Fung, Samantha Jane, Weickert, Cynthia Shannon, Newell, Kelly Anne. 2015. Alterations of mGluR5 and its endogenous regulators Norbin, Tamalin and Preso1 in schizophrenia: towards a model of mGluR5 dysregulation. In Acta neuropathologica, 130, 119-29. doi:10.1007/s00401-015-1411-6. https://pubmed.ncbi.nlm.nih.gov/25778620/
4. DiFrancesco, Jacopo C, Castellotti, Barbara, Milanesi, Raffaella, Granata, Tiziana, Gellera, Cinzia. 2019. HCN ion channels and accessory proteins in epilepsy: genetic analysis of a large cohort of patients and review of the literature. In Epilepsy research, 153, 49-58. doi:10.1016/j.eplepsyres.2019.04.004. https://pubmed.ncbi.nlm.nih.gov/30986657/
5. Dedoni, Simona, Olianas, Maria C, Ingianni, Angela, Onali, Pierluigi. 2016. Interferon-β Inhibits Neurotrophin 3 Signalling and Pro-Survival Activity by Upregulating the Expression of Truncated TrkC-T1 Receptor. In Molecular neurobiology, 54, 1825-1843. doi:10.1007/s12035-016-9789-2. https://pubmed.ncbi.nlm.nih.gov/26887385/
6. Kimura, Kouji, Kitano, Jun, Nakajima, Yoshiaki, Nakanishi, Shigetada. . Hyperpolarization-activated, cyclic nucleotide-gated HCN2 cation channel forms a protein assembly with multiple neuronal scaffold proteins in distinct modes of protein-protein interaction. In Genes to cells : devoted to molecular & cellular mechanisms, 9, 631-40. doi:. https://pubmed.ncbi.nlm.nih.gov/15265006/
7. Timms, Andrew E, Dorschner, Michael O, Wechsler, Jeremy, Horwitz, Marshall S, Tsuang, Debby W. . Support for the N-methyl-D-aspartate receptor hypofunction hypothesis of schizophrenia from exome sequencing in multiplex families. In JAMA psychiatry, 70, 582-90. doi:10.1001/jamapsychiatry.2013.1195. https://pubmed.ncbi.nlm.nih.gov/23553203/