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相关概念视频

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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针对向蛋白质O-GlcNAcylation的合体导向的自组合合体.

Zhihao Guo1, Tongyang Xu1, Khadija Shahed Khan1,2

  • 1Guangdong-Hong Kong-Macao Joint Laboratory for New Drug Screening, School of Pharmacy, The Chinese University of Hong Kong, Sha Tin, Hong Kong.

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概括
此摘要是机器生成的。

科学家们开发了一种新的O-GlcNAcylation向金马 (OGTAC),以精确控制蛋白质O-GlcNAcylation. 这种方法共性地利用O-GlcNAc转移酶 (OGT) 来修改特定的基质,为细胞信号研究提供了一种多功能工具.

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科学领域:

  • 生物化学 生化学
  • 分子生物学分子生物学
  • 化学生物学 化学生物学

背景情况:

  • 蛋白O-GlcNAcylation对于细胞信号传递至关重要,但很难精确控制.
  • 目前用于向O-GlcNAcylation的现有方法由于缺乏合适的O-GlcNAc转移酶 (OGT) 配体而受到限制.
  • 化学诱导近距离 (CIP) 是一种有前途的方法,用于向蛋白质的修饰.

研究的目的:

  • 开发一种新的方法,用于精确的,蛋白质特异的O-GlcNAcylation控制在活细胞中.
  • 创建一个非抑制的共价探针用于OGT使用联体导向释放 (LDR) 化学.
  • 设计一个自组装的O-GlcNAcylation Targeting Chimera (OGTAC),用于有针对性的OGT招聘.

主要方法:

  • 通过LDR化学,将一个强大的OGT抑制剂转化为一种非抑制性的共价探针.
  • 设计和建造一个自组装的OGTAC脚手架.
  • 在活细胞中应用OGTAC以准甲酶IIα (CK2α) 的O-GlcNAcylation.

主要成果:

  • 开发了新的配体,在保持其酶活性的同时对OGT进行共价标记.
  • 成功设计了一个自组装的OGTAC,它将OGT招募到其原生基质CK2α.
  • 在没有影响全球修饰水平的情况下,在细胞中实现了CK2α O-GlcNAcylation的选择性升高.

结论:

  • 引入了一种新的自我组装嵌合体类别,用于共价OGT参与和特定蛋白质O-GlcNAcylation.
  • 展示了一个多功能平台,用于剖析和控制O-GlcNAc在生物系统中的信号传输.
  • 为下一代OGTAC和针对O-GlcNAc调节的治疗策略铺平了道路.