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相关概念视频

Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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PI3K/mTOR/AKT Signaling Pathway01:22

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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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多个E3链酶控制着坦基拉酶的稳定性和功能.

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    此摘要是机器生成的。

    研究人员发现,RING-UIM E3酶通过促进K11无处不在,反对降解来稳定坦基酶. 这一发现为坦基拉酶调节和坦基拉酶抑制剂的潜在癌症治疗应用提供了新的见解.

    科学领域:

    • 生物化学 生物化学

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  • 分子生物学分子生物学
  • 癌症研究 癌症研究
  • 背景情况:

    • 坦基酶 (TNKS) 是ADP-ribosyltransferases,对于端粒凝聚力和Wnt/β-catenin信号传递至关重要.
    • 坦基酶的活性由聚-ADP-ribose (PAR) 和PAR结合E3链酶 (如RNF146) 调节,该链酶向PARylated蛋白质进行降解.
    • 小分子坦基拉酶抑制剂正在进行癌症治疗的研究.

    结论:

    • 发现了一种针对坦基拉酶的新型K11无处不在机制,可以对抗K48相关的降解.
    • 确定了多个参与调节坦基拉酶无处不在的PAR结合E3链酶.
    • 这些发现为坦基酶调节提供了新的见解,并建议在癌症治疗中使用坦基酶抑制剂的新疗法策略.