在VAMP721的Longin域内的氨酸酸开关调节SNARE功能
Martiniano Maria Ricardi1,2,3, Niklas Wallmeroth4, Cecilia Cermesoni2,3
1Ruhr University Bochum, Faculty of Biology and Biotechnology, Bochum, Germany.
The Plant journal : for cell and molecular biology
|September 2, 2023
概括
在 Tyrosine57 中对 VAMP721 的酸化调节了它在膜融合中的功能. 这种酸化控制了VAMP721的活性,这对分泌和植物发育至关重要.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 植物科学 植物科学
背景情况:
- 在分泌过程中,膜融合依赖于SNARE蛋白质,形成跨SNARE复合体.
- 监管域,如R-SNARE (VAMP) 中的Longin域 (LD),控制SNARE功能和本地化.
研究的目的:
- 调查VAMP721 Tyrosine57酸化在调节其功能的作用.
- 阐明VAMP721酸化对分泌,植物发育和蛋白质稳定性的影响.
主要方法:
- 使用了细胞生物学和遗传分析.
- 研究了阿斯巴酸盐突变 (模仿酸化) 和Y57F突变 (非酸化) 的影响.
- 在野生型植物中评估了vamp721vamp722功能丧失突变体和主导阴性表型的救援.
主要成果:
- 酸化模仿 (D) 导致VAMP721的不稳定性和降解.
- Y57F突变需要更高的剂量来拯救,这表明酸化调节SNARE功能.
- 突变VAMP721诱导主导负效应,导致聚合物并干扰根生长,分泌和细胞动力学.
结论:
- 铁素57酸化是VAMP721活动的关键调节步骤.
- 酸化促进了VAMP721的开放状态,促进了与SNARE合作伙伴进行膜融合的相互作用.
- 这种调节机制对于植物的正常分泌和发育至关重要.
相关概念视频
SNAREs and Membrane Fusion
11.0K
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...
11.0K
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
Pinching-off of Coated Vesicles
3.2K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.2K
Tail-anchoring of Proteins in the ER Membrane
3.1K
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...
3.1K
ATP Synthase: Structure
12.6K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
12.6K
Protein Translocation Machinery on the ER Membrane
4.7K
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...
4.7K


