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1
Molecular analysis of the X11-mLin-2/CASK complex in brain.大脑中X11-mLin-2/CASK复合物的分子分析。
J Neurosci. 1999 Feb 15;19(4):1307-16. doi: 10.1523/JNEUROSCI.19-04-01307.1999.
2
Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting.鉴定参与蛋白质靶向的进化保守异源三聚体蛋白复合物。
J Biol Chem. 1998 Nov 27;273(48):31633-6. doi: 10.1074/jbc.273.48.31633.
3
A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia.哺乳动物Lin-2/CASK的一种新型保守蛋白-蛋白相互作用结构域与SAP97结合，并将其招募至上皮细胞的侧面。
Mol Cell Biol. 2002 Mar;22(6):1778-91. doi: 10.1128/MCB.22.6.1778-1791.2002.
4
CASK participates in alternative tripartite complexes in which Mint 1 competes for binding with caskin 1, a novel CASK-binding protein.CASK参与了替代性三方复合物的形成，其中Mint 1与一种新型CASK结合蛋白caskin 1竞争结合。
J Neurosci. 2002 Jun 1;22(11):4264-73. doi: 10.1523/JNEUROSCI.22-11-04264.2002.
5
mLin-7 is localized to the basolateral surface of renal epithelia via its NH(2) terminus.mLin-7通过其氨基末端定位于肾上皮细胞的基底外侧表面。
Am J Physiol Renal Physiol. 2000 Mar;278(3):F464-75. doi: 10.1152/ajprenal.2000.278.3.F464.
6
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2.膜相关鸟苷酸激酶CASK/LIN-2的核转位与转录调控
Nature. 2000 Mar 16;404(6775):298-302. doi: 10.1038/35005118.
7
Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses.CASK/LIN-2与多配体蛋白聚糖硫酸乙酰肝素蛋白聚糖的直接相互作用及其在神经元突触中的重叠分布。
J Cell Biol. 1998 Jul 13;142(1):139-51. doi: 10.1083/jcb.142.1.139.
8
Lin-7 targets the Kir 2.3 channel on the basolateral membrane via a L27 domain interaction with CASK.Lin-7通过与CASK的L27结构域相互作用，将Kir 2.3通道靶向到基底外侧膜上。
Am J Physiol Cell Physiol. 2007 Dec;293(6):C1733-41. doi: 10.1152/ajpcell.00323.2007. Epub 2007 Oct 3.
9
Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells.人类CASK/LIN-2与syndecan-2和蛋白4.1结合，并定位于上皮细胞的基底外侧膜。
J Cell Biol. 1998 Jul 13;142(1):129-38. doi: 10.1083/jcb.142.1.129.
10
Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK.质膜Ca2+泵4b/CI与Ca2+/钙调蛋白依赖性膜相关激酶CASK的相互作用。
J Biol Chem. 2003 Mar 14;278(11):9778-83. doi: 10.1074/jbc.M212507200. Epub 2003 Jan 2.

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Nanoscale regulation of Ca dependent phase transitions and real-time dynamics of SAP97/hDLG.纳米尺度调控钙依赖性相转变和 SAP97/hDLG 的实时动态。
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2
Functional analysis of CASK transcript variants expressed in human brain.人脑中转录变体 CASK 的功能分析。
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3
Golgi localization of the LIN-2/7/10 complex points to a role in basolateral secretion of LET-23 EGFR in the vulval precursor cells.LIN-2/7/10 复合物的高尔基定位指向其在 尾部表皮细胞中基底外侧分泌 LET-23 EGFR 的作用。
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Exploring the Extended Biological Functions of the Human Copper Chaperone of Superoxide Dismutase 1.探索人类超氧化物歧化酶 1 的铜伴侣蛋白的扩展生物学功能。
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APP Protein Family Signaling at the Synapse: Insights from Intracellular APP-Binding Proteins.突触处的APP蛋白家族信号传导：来自细胞内APP结合蛋白的见解
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6
Intercellular protein-protein interactions at synapses.突触处的细胞间蛋白质-蛋白质相互作用。
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7
A matter of balance: role of neurexin and neuroligin at the synapse.平衡的问题：神经连接素和神经黏连蛋白在突触中的作用。
Neurochem Res. 2013 Jun;38(6):1174-89. doi: 10.1007/s11064-013-1029-9. Epub 2013 Apr 5.
8
CASK (LIN2) interacts with Cx43 in wounded skin and their coexpression affects cell migration.CASK（LIN2）与受伤皮肤中的 Cx43 相互作用，它们的共表达会影响细胞迁移。
J Cell Sci. 2012 Feb 1;125(Pt 3):695-702. doi: 10.1242/jcs.084400.
9
The molecular basis of the Caskin1 and Mint1 interaction with CASK.Caskin1 和 Mint1 与 CASK 相互作用的分子基础。
J Mol Biol. 2011 Sep 9;412(1):3-13. doi: 10.1016/j.jmb.2011.07.005. Epub 2011 Jul 12.
10
An X11alpha/FSBP complex represses transcription of the GSK3beta gene promoter.X11alpha/FSBP复合物抑制糖原合成酶激酶3β（GSK3β）基因启动子的转录。
Neuroreport. 2010 Aug 4;21(11):761-6. doi: 10.1097/WNR.0b013e32833bfca0.

本文引用的文献

1
Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein.胞质衔接蛋白与神经元载脂蛋白E受体及淀粉样前体蛋白的相互作用。
J Biol Chem. 1998 Dec 11;273(50):33556-60. doi: 10.1074/jbc.273.50.33556.
2
Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting.鉴定参与蛋白质靶向的进化保守异源三聚体蛋白复合物。
J Biol Chem. 1998 Nov 27;273(48):31633-6. doi: 10.1074/jbc.273.48.31633.
3
A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain.一种具有将脑内突触小泡胞吐作用与细胞黏附相偶联潜力的三方蛋白质复合体。
Cell. 1998 Sep 18;94(6):773-82. doi: 10.1016/s0092-8674(00)81736-5.
4
The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells.LIN-2/LIN-7/LIN-10复合物介导秀丽隐杆线虫表皮生长因子受体LET-23在外阴上皮细胞基底外侧膜的定位。
Cell. 1998 Sep 18;94(6):761-71. doi: 10.1016/s0092-8674(00)81735-3.
5
LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia.LIN-10是神经元和上皮细胞中极化蛋白定位途径的一个共享成分。
Cell. 1998 Sep 18;94(6):751-9. doi: 10.1016/s0092-8674(00)81734-1.
6
Regulation of nitric oxide synthase messenger RNA expression in the rat hippocampus by glucocorticoids.糖皮质激素对大鼠海马中一氧化氮合酶信使核糖核酸表达的调节
Neuroscience. 1998 Nov;87(2):439-46. doi: 10.1016/s0306-4522(98)00075-x.
7
A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins.一种与N-甲基-D-天冬氨酸受体和神经元细胞粘附蛋白相互作用的新型含多个PDZ结构域的分子。
J Biol Chem. 1998 Aug 14;273(33):21105-10. doi: 10.1074/jbc.273.33.21105.
8
Coordination of an array of signaling proteins through homo- and heteromeric interactions between PDZ domains and target proteins.通过PDZ结构域与靶蛋白之间的同聚和异聚相互作用来协调一系列信号蛋白。
J Cell Biol. 1998 Jul 27;142(2):545-55. doi: 10.1083/jcb.142.2.545.
9
Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses.CASK/LIN-2与多配体蛋白聚糖硫酸乙酰肝素蛋白聚糖的直接相互作用及其在神经元突触中的重叠分布。
J Cell Biol. 1998 Jul 13;142(1):139-51. doi: 10.1083/jcb.142.1.139.
10
Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells.人类CASK/LIN-2与syndecan-2和蛋白4.1结合，并定位于上皮细胞的基底外侧膜。
J Cell Biol. 1998 Jul 13;142(1):129-38. doi: 10.1083/jcb.142.1.129.

大脑中X11-mLin-2/CASK复合物的分子分析。

Molecular analysis of the X11-mLin-2/CASK complex in brain.

作者信息

Borg J P, Lõpez-Figueroa M O, de Taddèo-Borg M, Kroon D E, Turner R S, Watson S J, Margolis B

机构信息

Howard Hughes Medical Institute, University of Michigan Medical Center, Ann Arbor, Michigan 48109, USA.

出版信息

J Neurosci. 1999 Feb 15;19(4):1307-16. doi: 10.1523/JNEUROSCI.19-04-01307.1999.

DOI:10.1523/JNEUROSCI.19-04-01307.1999
PMID:9952408
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6786035/
Abstract

A heterotrimeric complex containing Lin-10/X11alpha, Lin-2/CASK, and Lin-7 is evolutionarily conserved from worms to mammals. In Caenorhabditis elegans, it localizes Let-23, a receptor tyrosine kinase, to the basolateral side of vulval epithelium, a step crucial for proper vulva development. In mammals, the complex may also participate in receptor targeting in neurons. Accordingly, phosphotyrosine binding (PTB) and postsynaptic density-95/Discs large/Zona Occludens-1 domains found in X11alpha and mLin-2/CASK bind to cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. In this paper, we have further analyzed the X11alpha-mLin-2/CASK association that is mediated by a novel protein-protein interaction. We show that the mLin-2/CASK calmodulin kinase II (CKII) domain directly binds to a 63 amino acids peptide located between the Munc-18-1 binding site and the PTB domain in X11alpha. Ca2+/calmodulin association with mLin-2/CASK does not modify the X11alpha-mLin-2 interaction. A region containing the mLin-2/CASK guanylate kinase domain also interacts with X11alpha but with a lower affinity than the CKII domain. Immunostaining of X11alpha in the brain shows that the protein is expressed in areas shown previously to be positive for mLin-2/CASK staining. Together, our data demonstrate that the X11alpha-mLin-2 complex contacts many partners, creating a macrocomplex suitable for receptor targeting at the neuronal plasma membrane.

摘要

包含Lin-10/X11α、Lin-2/CASK和Lin-7的异源三聚体复合物在从线虫到哺乳动物的进化过程中保守存在。在秀丽隐杆线虫中，它将受体酪氨酸激酶Let-23定位到外阴上皮的基底外侧，这是外阴正常发育的关键步骤。在哺乳动物中，该复合物也可能参与神经元中的受体靶向。因此，在X11α和mLin-2/CASK中发现的磷酸酪氨酸结合（PTB）和突触后密度95/盘状大蛋白/紧密连接蛋白1结构域与细胞表面蛋白结合，包括淀粉样前体蛋白、神经连接蛋白和多配体蛋白聚糖。在本文中，我们进一步分析了由新型蛋白质-蛋白质相互作用介导的X11α-mLin-2/CASK相互作用。我们发现mLin-2/CASK钙调蛋白激酶II（CKII）结构域直接与位于X11α中Munc-18-1结合位点和PTB结构域之间的一段63个氨基酸的肽段结合。Ca2+/钙调蛋白与mLin-2/CASK的结合并不改变X11α-mLin-2的相互作用。包含mLin-2/CASK鸟苷酸激酶结构域的区域也与X11α相互作用，但亲和力低于CKII结构域。大脑中X11α的免疫染色显示，该蛋白在先前显示mLin-2/CASK染色呈阳性的区域表达。总之，我们的数据表明X11α-mLin-2复合物与许多伙伴接触，形成了一个适合在神经元质膜上进行受体靶向的大复合物。