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• W2566099488 abstract "EFhd2/Swiprosin-1 is a cytoskeletal Ca2+-binding protein implicated in Ca2+-dependent cell spreading and migration in epithelial cells. EFhd2 domain architecture includes an N-terminal disordered region, a PxxP motif, two EF-hands, a ligand mimic helix and a C-terminal coiled-coil domain. We reported previously that EFhd2 displays F-actin bundling activity in the presence of Ca2+ and this activity depends on the coiled-coil domain and direct interaction of the EFhd2 core region. However, the molecular mechanism for the regulation of F-actin binding and bundling by EFhd2 is unknown. Here, the Ca2+-bound crystal structure of the EFhd2 core region is presented and structures of mutants defective for Ca2+-binding are also described. These structures and biochemical analyses reveal that the F-actin bundling activity of EFhd2 depends on the structural rigidity of F-actin binding sites conferred by binding of the EF-hands to Ca2+. In the absence of Ca2+, the EFhd2 core region exhibits local conformational flexibility around the EF-hand domain and C-terminal linker, which retains F-actin binding activity but loses the ability to bundle F-actin. In addition, we establish that dimerisation of EFhd2 via the C-terminal coiled-coil domain, which is necessary for F-actin bundling, occurs through the parallel coiled-coil interaction." @default.
• W2566099488 created "2017-01-06" @default.
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• W2566099488 date "2016-12-01" @default.
• W2566099488 modified "2023-10-16" @default.
• W2566099488 title "Structural implications of Ca2+-dependent actin-bundling function of human EFhd2/Swiprosin-1" @default.
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• W2566099488 doi "https://doi.org/10.1038/srep39095" @default.
• W2566099488 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5156911" @default.
• W2566099488 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27974828" @default.
• W2566099488 hasPublicationYear "2016" @default.
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