动胺相关蛋白1的交织关系,线粒体代谢和昼夜节律
Indrani Paramasivan Latha Laxmi1, Anica Tholath Job2, Venkatraman Manickam1
1School of Bio Sciences and Technology, Vellore Institute of Technology, Vellore, 632104, Tamil Nadu, India.
Molecular biology reports
|April 5, 2024
概括
由DRP1调节的线粒体动力学与昼夜节律有关. 失调会破坏新陈代谢健康,突出显示系统性疾病的潜在治疗点.
科学领域:
- 生物医学研究生物医学研究
- 线粒体生物学 线粒体生物学
- 时间生物学 时间生物学
背景情况:
- 线粒体对人类健康和衰老至关重要.
- 线粒体动力学受到昼夜钟基因的影响.
- 循环节律的扰乱会对代谢健康产生负面影响.
研究的目的:
- 审查DRP1-介导的线粒体动态和昼夜节律之间的关系.
- 探索这种关系对代谢途径的影响.
- 为了确定潜在的治疗策略,相关的健康问题.
主要方法:
- 目前研究的文献综述.
- 对DRP1在线粒体动态中的作用的分析.
- 探索昼夜节律对代谢健康的影响.
主要成果:
- DRP1介导的线粒体动力学与昼夜节律密切相关.
- 昼夜节律的失调会导致不良的代谢效应.
- 这种相互作用会影响各种代谢途径.
结论:
- 了解DRP1和昼夜节律之间的双向关系是关键.
- 针对这种相互作用可能为代谢和系统性疾病提供治疗益处.
相关概念视频
Circadian Rhythms and Gene Regulation
4.0K
The biological clock is involved in many aspects of regulating complex physiology in all animals. It was in 1935 when German zoologists, Hans Kalmus and Erwin Bünning, discovered the existence of circadian rhythm in Drosophila melanogaster. However, the internal molecular mechanisms behind the circadian clock remained a mystery until 1984, when Jeffrey C. Hall, Michael Rosbash, and Michael W. Young discovered the expression of the Per gene oscillating over a 24-hour cycle. In subsequent...
4.0K
Mitochondrial Membranes
10.2K
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
10.2K
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
The Inner Mitochondrial Membrane
3.3K
The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria. In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
3.3K
Mitochondrial Protein Sorting
4.3K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death. Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
4.3K
Energy to Drive Translocation
2.1K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
2.1K


