在Toxoplasma gondii的内细胞贩运中解读蛋白质化
Vern B Carruthers1, Zhicheng Dou2
1Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan, USA.
mBio
|February 26, 2024
概括
蛋白质化,一种膜定过程,对于Toxoplasma gondii来说至关重要,以传输宿主蛋白质. 这种机制也影响了寄生虫分泌器官的功能,提供了潜在的治疗点.
科学领域:
- 细胞生物学 细胞生物学
- 寄生虫学的寄生虫学
- 分子生物学分子生物学
背景情况:
- 毒素菌是一种细胞内原生虫寄生虫,侵入宿主细胞.
- 寄生虫内部化宿主蛋白质,以获得自己的资源和复制.
- 关于控制这些宿主衍生物质的细胞内贩运的分子机制的知识有限.
研究的目的:
- 为了研究分子决定因素,规范内细胞化宿主蛋白在Toxoplasma gondii内的贩运.
- 探索蛋白质化在这个贩运过程中的作用.
- 了解寄生虫生物学中关键识别蛋白质的更广泛的功能.
主要方法:
- 该研究涉及识别和表征参与宿主蛋白贩运的蛋白质.
- 研究了蛋白质前化的作用,后翻译性修改,在定蛋白质到膜.
- 利用分子和遗传方法来评估已识别的蛋白质的功能,包括Toxoplasma gondii Rab1B (TgRab1).
主要成果:
- 蛋白质先化被确定为对T. gondii. 内细胞化宿主蛋白的贩运至关重要.
- 发现Rab1B (TgRab1) 的一个必不可少的T. gondii ortolog参与了这种内细胞贩运途径.
- 此外,TgRab1在流通用于动物分泌器官的蛋白质方面也发挥着关键作用,在内细胞和外细胞通路中显示出双重功能.
结论:
- 蛋白质化对于T. gondii的细胞内蛋白质贩运至关重要,影响了内细胞和外细胞.
- 在内细胞和外细胞蛋白质运输中,TgRab1具有双重作用,这突显了它在寄生虫生物学中的重要性.
- 这些发现为进一步研究T. gondii内膜贩运开辟了道路,并建议蛋白质化作为潜在的治疗点.
相关概念视频
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
Mitochondrial Precursor Proteins
2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
Most of the mitochondrial...
2.6K
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
Protein Transport to the Outer Chloroplast Membrane
2.0K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
2.0K
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
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


