合成素集群和胆固醇会影响合成素1aa的移动性
Alan W Weisgerber1, Zdeněk Otruba1, Michelle K Knowles1
1Department of Chemistry and Biochemistry, University of Denver, Denver, Colorado.
Biophysical journal
|January 15, 2024
概括
合成素1a (Syx1a) 集群对于外细胞形成至关重要. 这项研究揭示了Syx1a分子在这些纳米域内更自由地移动,这种移动性取决于胆固醇和N终端Habc域的正常细胞功能.
科学领域:
- 细胞生物学 细胞生物学
- 神经科学是一个神经科学.
- 生物物理学的生物物理.
背景情况:
- 合成素1a (Syx1a) 对于神经内分泌细胞的表细胞形成至关重要.
- Syx1a在等离子膜上形成纳米级域,对于囊泡对接至关重要,但在聚变过程中分解.
- 这些纳米领域内Syx1a分子的动态平衡尚未完全理解.
研究的目的:
- 为了阐明Syx1a分子相对于集群位置的动态.
- 了解Syx1a集群如何保持其平衡以及分子如何在其中移动.
- 研究N端Habc域和胆固醇在Syx1a动态和外细胞形成中的作用.
主要方法:
- 开发了一种标记策略,可在PC12细胞上同时可视化批量Syx1a集群和跟踪单个Syx1a分子轨迹.
- 追踪了与集群位置相关的单个Syx1a分子运动.
- 利用模拟来模拟集群中的Syx1a动态.
主要成果:
- Syx1a分子在等离子体膜上表现出移动性,在集群中心具有更高的移动性,在集群边缘具有减少的移动性.
- N端 Habc 域和胆固醇对于这种移动性和适当的外细胞形成至关重要.
- 模拟支持一个由大型子维护的Syx1a星团模型,在更小的半径内具有高流动性.
- 胆固醇消耗显著降低了Syx1a在集群中的移动性.
结论:
- Syx1a集群动力学受到分子运动的影响,N端Habc域和胆固醇具有特定的作用.
- 一个子扩散模型解释了纳米领域内观察到的Syx1a动态.
- 血的流动性,特别是在Syx1a超分子中,对于外细胞功能至关重要.
相关概念视频
Vesicular Tubular Clusters
2.5K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
2.5K
Overview of Secretory Vesicles
8.5K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
8.5K
Fusion of Secretory Vesicles with the Plasma Membrane
11.1K
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.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
11.1K
Regulation of Nuclear Protein Sorting
2.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.4K
Translocation of Proteins into the Mitochondria
3.1K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.1K
SNAREs and Membrane Fusion
10.9K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
10.9K


