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Updated: Nov 8, 2025

Isolation of CA1 Nuclear Enriched Fractions from Hippocampal Slices to Study Activity-dependent Nuclear Import of Synapto-nuclear Messenger Proteins
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截然不同的活性区蛋白机械介导Ca2+道聚类和囊泡在海马突触中的初始化

Javier Emperador-Melero1, Jonathan W Andersen1, Sarah R Metzbower2

  • 1Department of Neurobiology, Harvard Medical School, Boston, MA, USA.

Nature neuroscience
|August 19, 2024
PubMed
概括

突触活性区使用单独的蛋白质机械来组织CaV2通道和启动囊泡. 林α和PTPσ蛋白对于在突触处组装囊泡起始部位至关重要.

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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