相关实验视频
Updated: Jul 3, 2026

11:27
Analysis of SCAP N-glycosylation and Trafficking in Human Cells
Published on: November 8, 2016
TRB3将E3无酸酶COP1与脂质代谢联系起来
Ling Qi1, Jose E Heredia, Judith Y Altarejos
1Peptide Biology Laboratories and Gene Expression Laboratories, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
概括
在禁食期间,Tribbles 3 (TRB3) 通过促进乙-辅酶A碳氧酶 (ACC) 降解来增强脂质分解. 这一发现揭示了维持能量平衡的新途径.
科学领域:
- 生物化学 生物化学
- 代谢调节 代谢调节 代谢调节 代谢调节
- 细胞生物学 细胞生物学
背景情况:
- 禁食触发了catecholamines通过乙-辅酶A碳酶 (ACC) 不活化来调动脂质.
- ACC是脂肪酸合成中的速度限制酶,对能量恒温至关重要.
研究的目的:
- 阐明一个平行途径,涉及Tribbles 3 (TRB3) 在禁食期间调节脂质代谢.
- 研究TRB3影响ACC活性和脂解的机制.
主要方法:
- 研究了TRB3在禁食期间脂肪组织中的作用.
- 研究了TRB3与构成性光形蛋白1 (COP1) 的相互作用及其对ACC无化的影响.
- 利用了TRB3缺乏脂肪细胞和转基因小鼠模型.
主要成果:
- 禁食期间TRB3的丰度增加,通过促进ACC降解来刺激脂解.
- TRB3通过与COP1的结合,促进了ACC的全域化,这是一种E3全域化酶.
- 缺乏TRB3的脂肪细胞显示ACC蛋白水平增加.
- 在脂肪组织中过度表达TRB3的转基因小鼠因脂肪酸氧化增强而不受饮食诱导的肥胖.
结论:
- 一个新的途径,TRB3介导的ACC降解在禁食期间有助于脂解和能量稳态.
- 酸化和无化途径汇聚在TRB3调节的ACC上,以控制脂质代谢.
- TRB3代表了管理肥胖和代谢障碍的潜在目标.
更多相关视频
相关概念视频
Cell Specific Gene Expression
Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
Cotranslational Protein Translocation
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Tail-anchoring of Proteins in the ER Membrane
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...
Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Post-translational Translocation of Proteins to the RER
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Lipid Catabolism
Triglycerides serve as crucial long-term energy storage molecules in microorganisms, providing a dense source of metabolic energy. Their breakdown is mediated by lipases, which hydrolyze triglycerides into glycerol and free fatty acids. Each of these components follows distinct metabolic pathways, ultimately contributing to ATP synthesis and cellular energy homeostasis.Glycerol MetabolismGlycerol, released from triglyceride hydrolysis, is phosphorylated by glycerol kinase to form...

