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草履虫刺激分泌偶联中的信号转导方面。

Aspects of signal transduction in stimulus exocytosis-coupling in Paramecium.

作者信息

Satir B H, Busch G, Vuoso A, Murtaugh T J

机构信息

Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461.

出版信息

J Cell Biochem. 1988 Apr;36(4):429-43. doi: 10.1002/jcb.240360411.

DOI:10.1002/jcb.240360411
PMID:2454239
Abstract

This paper deals with the detailed mechanisms of signal transduction that lead to exocytosis during regulative secretion induced by specific secretagogues in a eukaryotic cell, Paramecium tetraurelia. There are at least three cellular compartments involved in the process: I) the plasma membrane, which contains secretagogue receptors and other transmembrane proteins, II) the cytoplasms, particularly in the region between the cell and secretory vesicle membranes, where molecules may influence interactions of the membranes, and III) the secretory vesicle itself. The ciliated protozoan Paramecium tetraurelia is very well suited for the study of signal transduction events associated with exocytosis because this eukaryotic cell contains thousands of docked secretory vesicles (trichocysts) below the cell membrane which can be induced to release synchronously when triggered with secretagogue. This ensures a high signal-to-noise ratio for events associated with this process. Upon release the trichocyst membrane fuses with the cell membrane and the trichocyst content undergoes a Ca2+-dependent irreversible expansion. Secretory mutants are available which are blocked at different points in the signal transduction pathway. Aspects of the three components mentioned above that will be discussed here include a) the properties of the vesicle content, its pH, and its membrane; b) the role of phosphorylation/dephosphorylation of a cytosolic 63-kilodalton (kDa)Mr protein in membrane fusion; and c) how influx of extracellular Ca2+ required for exocytosis may take place via exocytic Ca2+ channels which may be associated with specific membrane microdomains (fusion rosettes).

摘要

本文探讨了在真核细胞四膜虫中,由特定促分泌素诱导的调节性分泌过程中导致胞吐作用的信号转导详细机制。该过程至少涉及三个细胞区室:I)质膜,其含有促分泌素受体和其他跨膜蛋白;II)细胞质,特别是在细胞与分泌囊泡膜之间的区域,分子可能在此影响膜的相互作用;III)分泌囊泡本身。纤毛原生动物四膜虫非常适合用于研究与胞吐作用相关的信号转导事件,因为这种真核细胞在细胞膜下方含有数千个停靠的分泌囊泡(刺丝泡),当用促分泌素触发时,这些囊泡可被诱导同步释放。这确保了与该过程相关事件的高信噪比。释放后,刺丝泡膜与细胞膜融合,刺丝泡内容物经历钙离子依赖性不可逆膨胀。存在在信号转导途径不同点被阻断的分泌突变体。这里将讨论的上述三个组分的方面包括:a)囊泡内容物的性质、其pH值及其膜;b)细胞质中一种63千道尔顿(kDa)蛋白质的磷酸化/去磷酸化在膜融合中的作用;c)胞吐作用所需的细胞外钙离子内流如何通过可能与特定膜微区(融合玫瑰花结)相关的胞吐钙离子通道发生。

相似文献

1
Aspects of signal transduction in stimulus exocytosis-coupling in Paramecium.草履虫刺激分泌偶联中的信号转导方面。
J Cell Biochem. 1988 Apr;36(4):429-43. doi: 10.1002/jcb.240360411.
2
Synchronous exocytosis in Paramecium cells. V. Ultrastructural adaptation phenomena during re-insertion of secretory organelles.草履虫细胞中的同步胞吐作用。V. 分泌细胞器重新插入过程中的超微结构适应现象。
Eur J Cell Biol. 1985 Jan;36(1):38-47.
3
Isolation of surface membranes from normal and exocytotic mutant strains of Paramecium tetraurelia. Ultrastructural and biochemical characterization.从四膜虫的正常和胞吐突变菌株中分离表面膜。超微结构和生化特性分析。
Eur J Cell Biol. 1981 Apr;24(1):108-15.
4
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J Eukaryot Microbiol. 2017 Jan;64(1):106-133. doi: 10.1111/jeu.12332. Epub 2016 Jul 18.
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Control of exocytotic processes: cytological and physiological studies of trichocyst mutants in Paramecium tetraurelia.胞吐过程的调控:四膜虫中刺丝泡突变体的细胞学与生理学研究
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Parafusin is a membrane and vesicle associated protein that cycles at exocytosis.副融合蛋白是一种与膜和囊泡相关的蛋白质,在胞吐作用中循环。
Eur J Cell Biol. 1998 Jan;75(1):46-53. doi: 10.1016/S0171-9335(98)80045-9.
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Cytoskeleton-secretory vesicle interactions during the docking of secretory vesicles at the cell membrane in Paramecium tetraurelia cells.四膜虫细胞中分泌囊泡在细胞膜对接过程中细胞骨架与分泌囊泡的相互作用。
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Molecular aspects of rapid, reversible, Ca2+-dependent de-phosphorylation of pp63/parafusin during stimulated exo-endocytosis in Paramecium cells.草履虫细胞受刺激的胞吐-胞吞作用过程中,pp63/副融合蛋白快速、可逆、Ca2+依赖的去磷酸化的分子机制。
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Trichocyst membrane fate in living Paramecium primaurelia visualized by multimodal confocal imaging.
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Membrane behavior of exocytic vesicles. II. Fate of the trichocyst membranes in Paramecium after induced trichocyst discharge.胞吐小泡的膜行为。II. 诱导刺丝泡释放后草履虫中刺丝泡膜的命运。
J Cell Biol. 1976 May;69(2):313-26. doi: 10.1083/jcb.69.2.313.

引用本文的文献

1
Lysozyme acts as a chemorepellent and secretagogue in Paramecium by activating a novel receptor-operated Ca++ conductance.溶菌酶通过激活一种新型的受体操纵性钙离子通道,在草履虫中充当化学排斥剂和促分泌素。
J Membr Biol. 1995 Nov;148(1):13-25. doi: 10.1007/BF00234152.
2
Cloning and sequencing of parafusin, a calcium-dependent exocytosis-related phosphoglycoprotein.副融合蛋白(一种与钙依赖性胞吐作用相关的磷酸糖蛋白)的克隆与测序
Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9832-6. doi: 10.1073/pnas.91.21.9832.
3
Species distribution of a phosphoprotein (parafusin) involved in exocytosis.
参与胞吐作用的一种磷蛋白(副融合蛋白)的物种分布。
Proc Natl Acad Sci U S A. 1989 Feb;86(3):930-2. doi: 10.1073/pnas.86.3.930.
4
Parafusin, an exocytic-sensitive phosphoprotein, is the primary acceptor for the glucosylphosphotransferase in Paramecium tetraurelia and rat liver.副融合蛋白是一种对胞吐敏感的磷蛋白,是四膜虫和大鼠肝脏中葡糖基磷酸转移酶的主要受体。
J Cell Biol. 1990 Sep;111(3):901-7. doi: 10.1083/jcb.111.3.901.
5
Quenched flow analysis of exocytosis in Paramecium cells: time course, changes in membrane structure, and calcium requirements revealed after rapid mixing and rapid freezing of intact cells.草履虫细胞胞吐作用的淬灭流分析:完整细胞快速混合和快速冷冻后揭示的时间进程、膜结构变化及钙需求
J Cell Biol. 1991 Jun;113(6):1295-304. doi: 10.1083/jcb.113.6.1295.
6
A Ca2+ influx associated with exocytosis is specifically abolished in a Paramecium exocytotic mutant.与胞吐作用相关的钙离子内流在草履虫胞吐突变体中被特异性消除。
J Cell Biol. 1990 Dec;111(6 Pt 1):2527-35. doi: 10.1083/jcb.111.6.2527.
7
The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release.蛋白激酶C及其神经元底物去磷酸化蛋白、B-50和富含丙氨酸的豆蔻酰化蛋白激酶C底物在神经递质释放中的作用。
Mol Neurobiol. 1991;5(2-4):87-130. doi: 10.1007/BF02935541.
8
Carbohydrate cycling in signal transduction: parafusin, a phosphoglycoprotein and possible Ca(2+)-dependent transducer molecule in exocytosis in Paramecium.信号转导中的碳水化合物循环:副融合蛋白,一种磷酸糖蛋白,可能是草履虫胞吐作用中Ca(2+)依赖的转导分子。
Proc Natl Acad Sci U S A. 1992 Dec 1;89(23):11297-301. doi: 10.1073/pnas.89.23.11297.