酸酶SHP2的调节和活性:SH2域,脱化活性,以及其他领域
1Department of Molecular Cell Biology, Institute for Cell Biology, University of Bonn, Bonn, 53115, Germany.
Biochemical Society transactions
|January 9, 2026
概括
含有酸酶-2 (SHP2) 的Src同质性2 (SH2) 域在癌症和RASopathies中至关重要. 最近的发现揭示了复杂的调节机制和新功能,指导了针对SHP2.2的未来治疗策略.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 细胞信号传递 细胞信号传递
背景情况:
- 含有Src同质2 (SH2) 域的酸酶-2 (SHP2) 是细胞信号通路中的关键调节剂.
- 在SHP2的突变与各种疾病有关,包括癌症和RASopathies.
- SHP2在促进细胞生长和抑制免疫细胞激活方面发挥着关键作用.
研究的目的:
- 审查野生型SHP2的调控机制,重点关注其SH2域和酸化.
- 突出了解SHP2的催化和非催化功能的最新进展.
- 讨论关于SHP2调节的新见解,包括SUMOylation和基质酸化.
主要方法:
- 关于SHP2.0的最新研究的文献综述.
- 分析SHP2的结构和功能.
- 影响SHP2活动的新兴监管途径的摘要.
主要成果:
- SHP2 调节涉及其 SH2 域和酸化的复杂相互作用.
- 对SHP2作为酸酶和适应器/支架蛋白的双重作用的新理解.
- 新兴的调节机制包括SUMOylation和受体独立激活.
结论:
- SHP2表现出复杂的监管网络,影响其功能.
- 最近的发现为深入了解SHP2的多方面作用提供了更深入的了解.
- 这些见解对于开发针对疾病的基于SHP2的向疗法至关重要.
相关概念视频
The JAK-STAT Signaling Pathway
11.9K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
11.9K
Protein Kinases and Phosphatases
14.9K
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...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
14.9K
Protein Kinases and Phosphatases
4.3K
4.3K
Phosphorylation
53.6K
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...
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...
53.6K
Amplifying Signals via Enzymatic Cascade
17.2K
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...
17.2K
Phosphoinositides and PIPs
10.1K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.1K


