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分泌囊泡的形态对接。

Morphological docking of secretory vesicles.

机构信息

Department of Functional Genomics, Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University Medical Center, VU University Amsterdam, 1081 HV Amsterdam, The Netherlands.

出版信息

Histochem Cell Biol. 2010 Aug;134(2):103-13. doi: 10.1007/s00418-010-0719-5. Epub 2010 Jun 26.

DOI:10.1007/s00418-010-0719-5
PMID:20577884
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2909457/
Abstract

Calcium-dependent secretion of neurotransmitters and hormones is essential for brain function and neuroendocrine-signaling. Prior to exocytosis, neurotransmitter-containing vesicles dock to the target membrane. In electron micrographs of neurons and neuroendocrine cells, like chromaffin cells many synaptic vesicles (SVs) and large dense-core vesicles (LDCVs) are docked. For many years the molecular identity of the morphologically docked state was unknown. Recently, we resolved the minimal docking machinery in adrenal medullary chromaffin cells using embryonic mouse model systems together with electron-microscopic analyses and also found that docking is controlled by the sub-membrane filamentous (F-)actin. Currently it is unclear if the same docking machinery operates in synapses. Here, I will review our docking assay that led to the identification of the LDCV docking machinery in chromaffin cells and also discuss whether identical docking proteins are required for SV docking in synapses.

摘要

钙依赖性神经递质和激素的分泌对于大脑功能和神经内分泌信号传导至关重要。在胞吐作用之前,含有神经递质的囊泡与靶膜对接。在神经元和神经内分泌细胞(如嗜铬细胞)的电子显微镜照片中,许多突触小泡(SVs)和大致密核心囊泡(LDCVs)都已对接。多年来,形态学对接状态的分子特征一直未知。最近,我们使用胚胎小鼠模型系统以及电子显微镜分析,解决了肾上腺髓质嗜铬细胞中的最小对接机制问题,还发现对接受亚膜丝状(F)-肌动蛋白的控制。目前尚不清楚相同的对接机制是否在突触中起作用。在这里,我将回顾导致鉴定嗜铬细胞中 LDCV 对接机制的对接测定法,并讨论在突触中 SV 对接是否需要相同的对接蛋白。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/044c76ef573c/418_2010_719_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/c805b51eb616/418_2010_719_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/856deefa3fec/418_2010_719_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/f21b236ef8d1/418_2010_719_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/3e3190781831/418_2010_719_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/044c76ef573c/418_2010_719_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/c805b51eb616/418_2010_719_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/856deefa3fec/418_2010_719_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/f21b236ef8d1/418_2010_719_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/3e3190781831/418_2010_719_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c17b/2909457/044c76ef573c/418_2010_719_Fig5_HTML.jpg

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