在膜上使用Sec18和Sec17的Qc-SNARE功能组件
Amy Orr1, Karina Lopes1, Jerry O'Dwyer1
1Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, 7200 Vail Building, Hanover, NH 03755.
Molecular biology of the cell
|November 19, 2025
概括
酵母真空聚变依赖于Sec17,Sec18,SNAREs和HOPS. 酵母真空聚变依赖于Sec17,Sec18,SNAREs和HOPS. 酵母真空聚变依赖于Sec17,Sec18,SNAREs和HOPS. 酵母真空聚变依赖于Sec17,Sec18,SNAREs和HOPS. 这项研究揭示了Qc-SNARE,Sec17和Sec18如何相互作用以推动聚变,澄清了Sec18的问题.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 酵母真空融合是细胞功能的一个关键过程.
- 融合是由包括Sec17,Sec18,SNAREs (R,Qa,Qb,Qc) 和HOPS复合体在内的蛋白质调解的.
- Sec18在催化聚变中的确切作用,特别是它与Qc-SNARE的相互作用,仍然不清楚.
研究的目的:
- 阐明Sec18促进酵母真空融合的机制.
- 为了研究Sec18,Sec17和Qc-SNARE之间的相互作用.
- 了解Sec18 ATPase活性在聚变调节中的作用.
主要方法:
- 生物化学测试用于研究蛋白质与蛋白质相互作用.
- 在SNARE和聚变机械的存在下分析Sec18 ATPase活性.
- 在试验室中化中间体的复制.
主要成果:
- Qc-SNARE对Sec17具有很高的亲和力,Sec18增强了这种相互作用.
- 一个四元复合体的膜结合的Qc:Sec18:Sec17被确定.
- Sec18 ATPase 解调节四元复合体和融合中的相互作用.
- Qc-SNARE显著刺激了Sec18 ATPase的活性.
结论:
- 提出了一个模型,其中膜结合的Qc:Sec17:Sec18复合体将HOPS从SNARE复合体中取代.
- 这种相互作用促进了完整的SNARE拉链,并利用Sec17在推动核聚变中的作用.
- Sec18作为一个关键调节器,通过其ATPase活性和与Qc-SNARE和Sec17的相互作用调节融合.
相关概念视频
SNAREs and Membrane Fusion
12.3K
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...
12.3K
Tail-anchoring of Proteins in the ER Membrane
3.7K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.7K
Assembly of Signaling Complexes
6.4K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.4K
Coat Assembly and GTPases
4.2K
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...
4.2K
Protein Translocation Machinery on the ER Membrane
6.5K
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
6.5K
Septins
2.2K
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...
2.2K


