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1
The dynamins: redundant or distinct functions for an expanding family of related GTPases?发动蛋白:对于一个不断扩展的相关GTP酶家族而言,其功能是冗余的还是独特的?
Proc Natl Acad Sci U S A. 1997 Jan 21;94(2):377-84. doi: 10.1073/pnas.94.2.377.
2
Functional analysis of dynamin isoforms in Drosophila melanogaster.黑腹果蝇中发动蛋白同工型的功能分析。
J Neurogenet. 1999 Nov;13(3):119-43. doi: 10.3109/01677069909083470.
3
Two isoforms of Drosophila dynamin in wild-type and shibire(ts) neural tissue: different subcellular localization and association mechanisms.野生型和发动蛋白温度敏感型(shibire(ts))神经组织中果蝇发动蛋白的两种同工型:不同的亚细胞定位和缔合机制。
J Neurogenet. 1995 Dec;10(3):169-91. doi: 10.3109/01677069509083462.
4
Dynamin II regulates hormone secretion in neuroendocrine cells.发动蛋白II调节神经内分泌细胞中的激素分泌。
J Biol Chem. 2001 Feb 9;276(6):4251-60. doi: 10.1074/jbc.M006371200. Epub 2000 Oct 13.
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Dynamin is a GTPase stimulated to high levels of activity by microtubules.发动蛋白是一种受微管刺激而达到高活性水平的GTP酶。
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6
Role of the basic, proline-rich region of dynamin in Src homology 3 domain binding and endocytosis.发动蛋白富含脯氨酸的碱性区域在Src同源3结构域结合及内吞作用中的作用。
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Differential expression and regulation of multiple dynamins.多种发动蛋白的差异表达与调控
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Induction of mutant dynamin specifically blocks endocytic coated vesicle formation.突变型发动蛋白的诱导特异性地阻断内吞被膜小泡的形成。
J Cell Biol. 1994 Nov;127(4):915-34. doi: 10.1083/jcb.127.4.915.
9
Genetic studies on dynamin function in Drosophila.果蝇中发动蛋白功能的遗传学研究。
J Neurogenet. 1993 Dec;9(2):73-87. doi: 10.3109/01677069309083451.
10
Association of a dynamin-like protein with the Golgi apparatus in mammalian cells.哺乳动物细胞中一种发动蛋白样蛋白与高尔基体的关联。
J Cell Biol. 1996 May;133(4):761-75. doi: 10.1083/jcb.133.4.761.

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Large-scale, dynamin-like motions of the human guanylate binding protein 1 revealed by multi-resolution simulations.多分辨率模拟揭示了人类鸟苷酸结合蛋白 1 的大规模、类似动力蛋白的运动。
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Dynasore inhibition on productive infection of HIV-1 in commonly used cell lines is independent of transferrin endocytosis.动力蛋白抑制剂对HIV-1在常用细胞系中的有效感染的抑制作用与转铁蛋白内吞作用无关。
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Justicidin A Reduces β-Amyloid via Inhibiting Endocytosis of β-Amyloid Precursor Protein.正义霉素A通过抑制β-淀粉样前体蛋白的内吞作用来减少β-淀粉样蛋白。
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Large G protein α-subunit XLαs limits clathrin-mediated endocytosis and regulates tissue iron levels in vivo.大 G 蛋白 α 亚基 XLαs 限制网格蛋白介导的内吞作用,并调节体内组织铁水平。
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10
Clathrin-dependent internalization, signaling, and metabolic processing of guanylyl cyclase/natriuretic peptide receptor-A.网格蛋白依赖的内化、信号转导和鸟苷酸环化酶/利钠肽受体-A 的代谢加工。
Mol Cell Biochem. 2018 Apr;441(1-2):135-150. doi: 10.1007/s11010-017-3180-0. Epub 2017 Sep 12.

本文引用的文献

1
Neurotransmitter release: fusion or 'kiss-and-run'?神经递质释放:融合还是“亲吻-逃离”?
Trends Cell Biol. 1994 Jan;4(1):1-4. doi: 10.1016/0962-8924(94)90025-6.
2
Endocytosis without clathrin.无网格蛋白的内吞作用
Trends Cell Biol. 1994 Aug;4(8):275-7. doi: 10.1016/0962-8924(94)90211-9.
3
Dynamin: a novel microtubule-associated GTPase.发动蛋白:一种新型的微管相关GTP酶。
Trends Cell Biol. 1991 Aug;1(2-3):57-60. doi: 10.1016/0962-8924(91)90090-v.
4
The regulation of endocytosis: identifying dynamin's binding partners.内吞作用的调控:确定发动蛋白的结合伴侣。
Trends Cell Biol. 1995 Feb;5(2):43-7. doi: 10.1016/s0962-8924(00)88937-0.
5
Three dynamin-encoding genes are differentially expressed in developing rat brain.三个动力蛋白编码基因在发育中的大鼠大脑中差异表达。
J Neurochem. 1996 Sep;67(3):927-31. doi: 10.1046/j.1471-4159.1996.67030927.x.
6
The synaptic vesicle cycle: a single vesicle budding step involving clathrin and dynamin.突触小泡循环:一个涉及网格蛋白和发动蛋白的单个小泡出芽步骤。
J Cell Biol. 1996 Jun;133(6):1237-50. doi: 10.1083/jcb.133.6.1237.
7
Association of a dynamin-like protein with the Golgi apparatus in mammalian cells.哺乳动物细胞中一种发动蛋白样蛋白与高尔基体的关联。
J Cell Biol. 1996 May;133(4):761-75. doi: 10.1083/jcb.133.4.761.
8
Sea urchin egg 100-kDa dynamin-related protein: identification of and localization to intracellular vesicles.海胆卵100千道尔顿动力蛋白相关蛋白:鉴定及其在细胞内囊泡中的定位
Dev Biol. 1993 Oct;159(2):581-94. doi: 10.1006/dbio.1993.1266.
9
The GTPase dynamin binds to and is activated by a subset of SH3 domains.GTP酶发动蛋白与SH3结构域的一个子集结合并被其激活。
Cell. 1993 Oct 8;75(1):25-36.
10
Caveolae and sorting in the trans-Golgi network of epithelial cells.上皮细胞反式高尔基体网络中的小窝与分选
EMBO J. 1993 Apr;12(4):1597-605. doi: 10.1002/j.1460-2075.1993.tb05804.x.

发动蛋白:对于一个不断扩展的相关GTP酶家族而言,其功能是冗余的还是独特的?

The dynamins: redundant or distinct functions for an expanding family of related GTPases?

作者信息

Urrutia R, Henley J R, Cook T, McNiven M A

机构信息

Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA.

出版信息

Proc Natl Acad Sci U S A. 1997 Jan 21;94(2):377-84. doi: 10.1073/pnas.94.2.377.

DOI:10.1073/pnas.94.2.377
PMID:9012790
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC34135/
Abstract

In the 7 years since dynamin was first isolated from bovine brain in search of novel microtubule-based motors, our understanding of this enzyme has expanded significantly. We now know that brain dynamin belongs to a family of large GTPases, which mediate vesicle trafficking. Furthermore, this enzymatic activity is markedly increased through association with microtubules, acidic phospholipids, and certain regulatory proteins that contain Src homology 3 (SH3) domains. From functional, genetic, and cellular manipulations, it is now generally accepted that dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event. These observations have confirmed at least one function of dynamin that was predicted from seminal studies on a pleiotropic mutant, shibire(ts) (shi(ts)) in Drosophila melanogaster. Of equal interest is the finding that there are multiple dynamin gene products, including two that are expressed in a tissue-specific manner, and they share marked homology with a larger family of distinct but related proteins. Therefore, it is attractive to speculate that the different dynamins may participate in related cellular functions, such as distinct endocytic processes and even secretion. In turn, dynamin could play an important role in cell growth, cell spreading, and neurite outgrowth. The purpose of this review is to enumerate on the expansive dynamin literature and to discuss the nomenclature, expression, and putative functions of this growing and interesting family of proteins.

摘要

自从为寻找新型基于微管的马达蛋白而首次从牛脑中分离出发动蛋白以来的7年里,我们对这种酶的理解有了显著扩展。我们现在知道,脑发动蛋白属于一个大GTP酶家族,该家族介导囊泡运输。此外,通过与微管、酸性磷脂以及某些含有Src同源3(SH3)结构域的调节蛋白结合,这种酶活性会显著增加。从功能、遗传和细胞操作方面来看,现在普遍认为发动蛋白在胞吐事件后参与受体、相关配体和质膜的内吞摄取。这些观察结果证实了发动蛋白的至少一项功能,这一功能是从对果蝇中一种多效性突变体——失活(温度敏感型)(shi(ts))的开创性研究中预测出来的。同样有趣的是,发现有多种发动蛋白基因产物,包括两种以组织特异性方式表达的产物,它们与一个更大的不同但相关的蛋白质家族有显著的同源性。因此,推测不同的发动蛋白可能参与相关的细胞功能,如不同的内吞过程甚至分泌,是很有吸引力的。反过来,发动蛋白可能在细胞生长、细胞铺展和神经突生长中发挥重要作用。这篇综述的目的是梳理关于发动蛋白的大量文献,并讨论这个不断发展且有趣的蛋白质家族的命名、表达和假定功能。