риботоксинα-sarcin与复杂模型脂质囊泡的相互作用
Carmen García-Montoya1, Sara García-Linares1, Diego Heras-Márquez1
1Departamento de Bioquímica y Biología Molecular, Universidad Complutense, Madrid, Spain.
Archives of biochemistry and biophysics
|November 24, 2023
概括
菌的核毒素,如α-sarcin,通过穿越细胞膜来向核糖体. 它们与包括胆固醇在内的复杂脂质膜的相互作用影响细胞特异性和毒素活性.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
背景情况:
- 菌核糖毒素是细胞外RNase,通过分裂rRNA,使核糖体失活.
- 这些毒素表现出细胞特异性,向瘤或感染病毒的细胞.
- 之前的研究表明, риботоксин与负电荷的膜相互作用.
研究的目的:
- 为了研究真菌 риботоксинα-sarcin与类似哺乳动物细胞膜的复杂脂质膜的相互作用.
- 阐明脂质组成的作用,包括sphingophospholipids和胆固醇,在α-sarcin的膜相互作用和细胞特异性.
主要方法:
- 使用野生型α-sarcin进行相互作用研究.
- 测试了α-sarcin对各种囊泡构成的影响,包括不同的脂类组,脂肪酸和度,乙烯链长度和胆固醇含量.
主要成果:
- α-sarcin的囊泡聚合对膜电荷密度,脂质头组和脂肪酸链和度敏感.
- 乙链的长度显著影响脂质的混合.
- 胆固醇通过稀释负电荷来调节α-sarcin的穿越膜的能力.
结论:
- 菌的利博毒素与细胞膜的相互作用是复杂的,并受到脂质成分的影响.
- 胆固醇在调节α-sarcin的膜透性和细胞向方面发挥着关键作用.
- 了解这些相互作用对于基于 риботоксин的治疗策略至关重要.
相关概念视频
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
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
Rab Proteins
3.9K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
3.9K
Rab Cascades
2.7K
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.
2.7K
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


