Regulatory mechanisms triggered by enzyme interactions with lipid membrane surfaces

被引:2
|
作者
Yu, Jie [1 ]
Boehr, David D. [1 ]
机构
[1] Penn State Univ, Dept Chem, University Pk, PA 16801 USA
基金
美国国家卫生研究院;
关键词
protein-membrane interactions; allosteric regulation; conformational change; signaling; lipid metabolism; lipid kinase; phosphatidylinositol phosphate lipids; PROTEIN-KINASE-C; FOCAL ADHESION KINASE; BINDING DOMAIN; SUBSTRATE-SPECIFICITY; PHOSPHOLIPASE A(2); STRUCTURAL BASIS; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; ALLOSTERIC ACTIVATION; AMPHIPATHIC HELIX; CRYSTAL-STRUCTURE;
D O I
10.3389/fmolb.2023.1306483
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Recruitment of enzymes to intracellular membranes often modulates their catalytic activity, which can be important in cell signaling and membrane trafficking. Thus, re-localization is not only important for these enzymes to gain access to their substrates, but membrane interactions often allosterically regulate enzyme function by inducing conformational changes across different time and amplitude scales. Recent structural, biophysical and computational studies have revealed how key enzymes interact with lipid membrane surfaces, and how this membrane binding regulates protein structure and function. This review summarizes the recent progress in understanding regulatory mechanisms involved in enzyme-membrane interactions.
引用
收藏
页数:12
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