• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

分子缝隙连接伴侣重塑调控缝隙连接运输:从生理学至病理生理学。

Molecular connexin partner remodeling orchestrates connexin traffic: from physiology to pathophysiology.

机构信息

INSERM U 1065, University Nice Sophia Antipolis, Team 5, C3M, 151 route Saint-Antoine de Ginestière, France.

出版信息

Crit Rev Biochem Mol Biol. 2012 Sep;47(5):407-23. doi: 10.3109/10409238.2012.683482. Epub 2012 May 3.

DOI:10.3109/10409238.2012.683482
PMID:22551357
Abstract

Connexins, through gap junctional intercellular communication, are known to regulate many physiological functions involved in developmental processes such as cell proliferation, differentiation, migration and apoptosis. Strikingly, alterations of connexin expression and trafficking are often, if not always, associated with human developmental diseases and carcinogenesis. In this respect, disrupted trafficking dynamics and aberrant intracytoplasmic localization of connexins are considered as typical features of functionality failure leading to the pathological state. Recent findings demonstrate that interactions of connexins with numerous protein partners, which take place throughout connexin trafficking, are essential for gap junction formation, membranous stabilization and degradation. In the present study, we give an overview of the physiological molecular machinery and of the specific interactions between connexins and their partners, which are involved in connexin trafficking, and we highlight their changes in pathological situations.

摘要

间隙连接蛋白通过缝隙连接细胞间通讯,已知可调节许多生理功能,如细胞增殖、分化、迁移和凋亡。值得注意的是,连接蛋白表达和运输的改变通常(如果不是总是)与人类发育性疾病和癌发生有关。在这方面,连接蛋白运输动力学的破坏和细胞内定位的异常被认为是导致病理状态的功能衰竭的典型特征。最近的研究结果表明,连接蛋白与许多蛋白伴侣的相互作用发生在连接蛋白运输的整个过程中,对于间隙连接的形成、膜的稳定和降解是必不可少的。在本研究中,我们概述了参与连接蛋白运输的生理分子机制和连接蛋白与其伴侣之间的特定相互作用,并强调了它们在病理情况下的变化。

相似文献

1
Molecular connexin partner remodeling orchestrates connexin traffic: from physiology to pathophysiology.分子缝隙连接伴侣重塑调控缝隙连接运输:从生理学至病理生理学。
Crit Rev Biochem Mol Biol. 2012 Sep;47(5):407-23. doi: 10.3109/10409238.2012.683482. Epub 2012 May 3.
2
Connexin 33 impairs gap junction functionality by accelerating connexin 43 gap junction plaque endocytosis.连接蛋白 33 通过加速连接蛋白 43 缝隙连接斑块内吞作用来损害缝隙连接功能。
Traffic. 2009 Sep;10(9):1272-85. doi: 10.1111/j.1600-0854.2009.00949.x. Epub 2009 May 27.
3
Regulation of gap junction intercellular communication by the ubiquitin system.泛素系统对缝隙连接细胞间通讯的调节。
Cell Signal. 2010 Sep;22(9):1267-73. doi: 10.1016/j.cellsig.2010.03.005. Epub 2010 Mar 4.
4
The gap junction proteome and its relationship to disease.间隙连接蛋白组及其与疾病的关系。
Trends Cell Biol. 2010 Feb;20(2):92-101. doi: 10.1016/j.tcb.2009.11.001. Epub 2009 Nov 26.
5
Retinal horizontal cell-specific promoter activity and protein expression of zebrafish connexin 52.6 and connexin 55.5.斑马鱼连接蛋白52.6和连接蛋白55.5的视网膜水平细胞特异性启动子活性及蛋白表达
J Comp Neurol. 2007 Apr 10;501(5):765-79. doi: 10.1002/cne.21282.
6
Gap junctions and cancer: new functions for an old story.间隙连接与癌症:旧故事中的新功能
Antioxid Redox Signal. 2009 Feb;11(2):323-38. doi: 10.1089/ars.2008.2153.
7
Connexins and their channels in cell growth and cell death.连接蛋白及其通道在细胞生长和细胞死亡中的作用。
Cell Signal. 2006 May;18(5):592-600. doi: 10.1016/j.cellsig.2005.08.012. Epub 2005 Sep 23.
8
[The role of intercellular communication via "gap junctions" in disease].[通过“间隙连接”进行细胞间通讯在疾病中的作用]
Ned Tijdschr Geneeskd. 2003 Dec 13;147(50):2463-6.
9
Plasma membrane channels formed by connexins: their regulation and functions.由连接蛋白形成的质膜通道:其调节与功能。
Physiol Rev. 2003 Oct;83(4):1359-400. doi: 10.1152/physrev.00007.2003.
10
Gap junctions: structure and function (Review).间隙连接:结构与功能(综述)
Mol Membr Biol. 2002 Apr-Jun;19(2):121-36. doi: 10.1080/09687680210139839.

引用本文的文献

1
Connexin Gap Junction Channels and Hemichannels: Insights from High-Resolution Structures.连接蛋白间隙连接通道和半通道:高分辨率结构带来的见解
Biology (Basel). 2024 Apr 26;13(5):298. doi: 10.3390/biology13050298.
2
Cooperative cell-cell actin network remodeling to perform Gap junction endocytosis.协同的细胞间肌动蛋白网络重塑以进行间隙连接内吞作用。
Basic Clin Androl. 2023 Aug 3;33(1):20. doi: 10.1186/s12610-023-00194-y.
3
Calmodulin Directly Interacts with the Cx43 Carboxyl-Terminus and Cytoplasmic Loop Containing Three ODDD-Linked Mutants (M147T, R148Q, and T154A) that Retain α-Helical Structure, but Exhibit Loss-of-Function and Cellular Trafficking Defects.
钙调蛋白直接与包含三个ODDD连接突变体(M147T、R148Q和T154A)的Cx43羧基末端和细胞质环相互作用,这些突变体保留α-螺旋结构,但表现出功能丧失和细胞运输缺陷。
Biomolecules. 2020 Oct 17;10(10):1452. doi: 10.3390/biom10101452.
4
Cx32 exerts anti-apoptotic and pro-tumor effects via the epidermal growth factor receptor pathway in hepatocellular carcinoma.Cx32 通过表皮生长因子受体通路在肝癌中发挥抗细胞凋亡和促肿瘤作用。
J Exp Clin Cancer Res. 2019 Apr 4;38(1):145. doi: 10.1186/s13046-019-1142-y.
5
Connexin43 Carboxyl-Terminal Domain Directly Interacts with β-Catenin.连接蛋白 43 C 端结构域直接与β-连环蛋白相互作用。
Int J Mol Sci. 2018 May 24;19(6):1562. doi: 10.3390/ijms19061562.
6
Protein⁻Protein Interactions with Connexin 43: Regulation and Function.蛋白与连接蛋白 43 的相互作用:调控与功能。
Int J Mol Sci. 2018 May 10;19(5):1428. doi: 10.3390/ijms19051428.
7
Chemical shift assignments of the connexin37 carboxyl terminal domain.连接蛋白37羧基末端结构域的化学位移归属
Biomol NMR Assign. 2017 Oct;11(2):137-141. doi: 10.1007/s12104-017-9735-x. Epub 2017 Mar 1.
8
Connexins: substrates and regulators of autophagy.连接蛋白:自噬的底物与调节因子
BMC Cell Biol. 2016 May 24;17 Suppl 1(Suppl 1):20. doi: 10.1186/s12860-016-0093-9.
9
Physiological roles of connexins and pannexins in reproductive organs.连接蛋白和泛连接蛋白在生殖器官中的生理作用。
Cell Mol Life Sci. 2015 Aug;72(15):2879-98. doi: 10.1007/s00018-015-1965-4. Epub 2015 Jun 23.
10
Extracellular vesicles as carriers of microRNA, proteins and lipids in tumor microenvironment.细胞外囊泡作为肿瘤微环境中微小RNA、蛋白质和脂质的载体
Int J Cancer. 2016 Jan 1;138(1):14-21. doi: 10.1002/ijc.29417. Epub 2015 Jan 23.