棕化对于Sept8-204和Sept5是必需的,以形成类似囊泡的结构,并与synaptophysin结合
Huicong Liu1,2, Rong Tan1,2, Jia Tong1,2
1The Second Affiliated Hospital of Xinxiang Medical University, Xinxiang, China.
Journal of cellular biochemistry
|February 3, 2024
概括
蛋白棕化对于Sept8-204/Sept5形成小囊泡并与synaptophysin相互作用至关重要. 这个由ZDHHC17和PPT1调节的过程对突触功能至关重要.
科学领域:
- 神经科学是一个神经科学.
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
背景情况:
- Sept8是一种囊泡相关蛋白质,具有两种小鼠大脑变体:Sept8-204和Sept8-201.
- 众所周知,Sept8经历了棕化,这是一个翻译后的修改.
研究的目的:
- 为了研究蛋白质棕化在Sept8功能中的作用.
- 确定Sept8变种如何与Sept5相互作用并影响囊泡结构.
- 为了确定调节Sept8棕化酶的酶.
主要方法:
- Sept8变种 (Sept8-204,Sept8-201) 与Sept5的同时表达.
- 非棕化Sept8-204突变体 (Sept8-204-3CA) 的表达.
- 使用2-棕酸盐 (2-BP) 抑制棕化.
- 囊泡结构的分析和用SYP (synaptophysin) 的局部化.
- 调查ZDHHC17和PPT1在Sept8棕细胞结合中的作用.
主要成果:
- Sept8-204/Sept5的共同表达形成了小囊泡,而Sept8-201/Sept5则形成了大点.
- 棕化Sept8-204对于小囊泡的形成和SYP的局部化至关重要.
- 非palmitoylated Sept8-204或palmitoylation 抑制导致大 puncta 和减少 SYP 的局部化.
- ZDHHC17的损失降低了Sept8-204的棕化,导致大点.
- PPT1的损失增加了Sept8-204的棕化,促进了小囊泡的形成.
结论:
- 蛋白质棕化对于维持Sept8-204/Sept5.5的小囊状结构至关重要.
- Sept8-204的动态棕化受ZDHHC17和PPT1.4的调节.
- 这些发现表明,Sept8棕化在突触功能中起着重要作用.
相关概念视频
Septins
1.8K
Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
1.8K
Coat Assembly and GTPases
3.5K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.5K
Role of Septins
1.8K
Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
1.8K
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
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
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


