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相关概念视频

Phosphorylation01:02

Phosphorylation

44.8K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
44.8K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
12.2K
The Unfolded Protein Response01:37

The Unfolded Protein Response

5.6K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
5.6K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

2.2K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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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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相关实验视频

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Xenopus laevis as a Model to Identify Translation Impairment
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Xenopus laevis as a Model to Identify Translation Impairment

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通过p90rsk对Erp1的酸化是Xenopus laevis蛋中细胞静态因子的停止所需的.

Tomoko Nishiyama1, Keita Ohsumi, Takeo Kishimoto

  • 1Laboratory of Cell and Developmental Biology, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.

Nature
|April 6, 2007
PubMed
概括
此摘要是机器生成的。

莫斯和Erp1/Emi2协作维持Xenopus蛋中的细胞静止因子 (CSF) 逮捕. 依赖莫斯的酸化稳定了Erp1/Emi2,增强了其抑制酶促进复合物/循环体 (APC/C) 的作用.

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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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科学领域:

  • 细胞生物学 细胞生物学
  • 发育生物学 发展生物学
  • 分子生物学分子生物学

背景情况:

  • 由于细胞静止因子 (CSF) 的作用,脊椎动物卵在二分化二代阶段停产.
  • 脑脊液活动抑制了亚纳相促进复合体/环体 (APC/C),防止了环素的降解.
  • Erp1/Emi2和Mos是参与建立和维持CSF逮捕的关键蛋白质.

研究的目的:

  • 为了澄清在CSF中Mos和Erp1/Emi2之间的关系.
  • 调查Erp1/Emi2.2的莫斯依赖酸化的作用.

主要方法:

  • 分析Erp1/Emi2作为Xenopus蛋提取物中p90rsk的基质.
  • 在CSF捕获的蛋提取物中对Erp1/Emi2活性进行半定量分析.
  • 调查Erp1/Emi2与APC/C销毁盒结合的情况.

主要成果:

  • 特定地点的p90rsk对Erp1/Emi2的莫斯依赖酸化对于稳定Erp1/Emi2和建立CSF捕获至关重要.
  • 酸化增强了Erp1/Emi2的活性,维持了基相停止,但没有产生它.
  • 摩斯依赖酸化增强了Erp1/Emi2与APC/C的结合,抑制了环林B的降解.

结论:

  • 莫斯和Erp1/Emi2一起工作,以建立和维持Xenopus蛋的第二阶段停止.
  • 这项研究提供了一种分子机制,将Mos和Erp1/Emi2连接起来,用于未受精的脊椎动物卵中的CSF捕获.