范格尔2的PDZ结合图案的PDZ范围和结构特征
Marta Montserrat-Gomez1, Gergo Gogl2, Kendall Carrasco3
1Aix Marseille Université, CNRS, INSERM, Institut Paoli-Calmettes, CRCM, Equipe labellisée Ligue 'Cell polarity, cell signaling and cancer', Marseille, France.
Biochimica et biophysica acta. Proteins and proteomics
|December 24, 2023
概括
这项研究揭示了VANGL2如何与PDZ蛋白相互作用,确定了关键的残留物和酸化位,这些残留物和酸化位调节了其在平面细胞极性通路中的结合特征.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- VANGL2对于非正规的Wnt/平面细胞极性 (PCP) 信号通路至关重要.
- 它通过其C端PDZ结合基因 (PBM) 与PDZ蛋白相互作用.
研究的目的:
- 为了全面描述VANGL2 PDZome-binding profile的特征. 为了全面描述VANGL2 PDZome-binding profile的特征. 为了全面描述VANGL2 PDZome-binding profile的特征. 为了全面描述VANGL2 PDZome-binding profile的特征. 为了全面描述VANGL2 PDZome-binding profile的特征. 为了全面描述VANGL2 PDZome-binding profile的特征.
- 调查特定的PBM残留物和酸化在VANGL2相互作用中的作用.
主要方法:
- 采用了包括保留试验在内的直角方法.
- 对VANGL2 PBM进行了切断和点突变分析.
- 使用了通过晶体学进行的结构分析.
主要成果:
- VANGL2与广泛的PDZ域互动,包括一些新的PDZ域.
- 超出正规P-0和P-2位置的残留物 (例如,E518,Q516,R514) 增强了结合强度.
- 对S517,T519和S520的酸化大大改变了VANGL2 PDZome的结合特征.
结论:
- 这项研究提供了VANGL2 PDZ互动组的广泛地图.
- 特定的PBM残留物和翻译后的修改极大地调节了VANGL2的结合能力.
- 这些发现将指导未来对PCP信号中的VANGL2功能的研究.
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