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- W2902800597 abstract "DSPs are found in all organisms, from bacteria to humans. DSPs function in membrane fission and fusion, bundling of microtubules, and during the innate immune response to microbes. Common structural features of DSPs include the presence of a globular GTPase domain with an adjacent α-helical bundle domain. The mechanochemical properties of DSPs are driven by GTP hydrolysis that results in conformational changes in the α-helical bundle domains. Different DSPs have unique features, such as distinct lipid-binding motifs and protein–protein interaction domains, which target them to specific sites where they perform specific functions. Dynamin superfamily proteins (DSPs) mediate membrane fission and fusion necessary for endocytosis, organelle biogenesis and maintenance, as well as for bacterial cytokinesis. They also function in the innate immune response to pathogens and in organizing the cytoskeleton. In this review, we summarize the current understanding of the molecular mechanism of DSPs, with emphasis on the structural basis of function. Studies from the past decade on the structure and mechanism of DSPs enable comparative analysis of shared mechanisms and unique features of this protein family. Dynamin superfamily proteins (DSPs) mediate membrane fission and fusion necessary for endocytosis, organelle biogenesis and maintenance, as well as for bacterial cytokinesis. They also function in the innate immune response to pathogens and in organizing the cytoskeleton. In this review, we summarize the current understanding of the molecular mechanism of DSPs, with emphasis on the structural basis of function. Studies from the past decade on the structure and mechanism of DSPs enable comparative analysis of shared mechanisms and unique features of this protein family." @default.
- W2902800597 created "2018-12-11" @default.
- W2902800597 creator A5068703722 @default.
- W2902800597 creator A5085060944 @default.
- W2902800597 date "2019-03-01" @default.
- W2902800597 modified "2023-10-15" @default.
- W2902800597 title "Structural Insights into the Mechanism of Dynamin Superfamily Proteins" @default.
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