Cryo-EM structures of membrane-bound dynamin in a post-hydrolysis state primed for membrane fission.

Autor: Jimah JR; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: jimah@princeton.edu., Kundu N; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA., Stanton AE; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA., Sochacki KA; Biochemistry and Biophysics Center, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA., Canagarajah B; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA., Chan L; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA., Strub MP; Biochemistry and Biophysics Center, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA., Wang H; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA., Taraska JW; Biochemistry and Biophysics Center, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA., Hinshaw JE; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: jennyh@niddk.nih.gov.

Publikováno v: Developmental cell [Dev Cell] 2024 Jul 22; Vol. 59 (14), pp. 1783-1793.e5. Date of Electronic Publication: 2024 Apr 24.

Local monomer levels and established filaments potentiate non-muscle myosin 2 assembly.

Autor: Quintanilla MA; Department of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, USA., Patel H; Department of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, USA., Wu H; Department of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, USA., Sochacki KA; Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA., Chandrasekar S; Department of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, USA., Akamatsu M; Department of Biology, University of Washington, Seattle, WA, USA., Rotty JD; Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, MD, USA., Korobova F; Feinberg School of Medicine, Northwestern University, Chicago, IL, USA., Bear JE; Department of Cell Biology and Physiology, University of North Carolina-Chapel Hill, Chapel Hill, NC, USA., Taraska JW; Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA., Oakes PW; Department of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, USA., Beach JR; Department of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, USA.

Publikováno v: The Journal of cell biology [J Cell Biol] 2024 Apr 01; Vol. 223 (4). Date of Electronic Publication: 2024 Feb 14.

A conformational switch in clathrin light chain regulates lattice structure and endocytosis at the plasma membrane of mammalian cells.

Autor: Obashi K; Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Building 50, Bethesda, MD, 20892, USA., Sochacki KA; Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Building 50, Bethesda, MD, 20892, USA., Strub MP; Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Building 50, Bethesda, MD, 20892, USA., Taraska JW; Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Building 50, Bethesda, MD, 20892, USA. justin.taraska@nih.gov.

Publikováno v: Nature communications [Nat Commun] 2023 Feb 09; Vol. 14 (1), pp. 732. Date of Electronic Publication: 2023 Feb 09.

Dual clathrin and integrin signaling systems regulate growth factor receptor activation.

Autor: Alfonzo-Méndez MA; Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Building 50, Bethesda, MD, 20892, USA., Sochacki KA; Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Building 50, Bethesda, MD, 20892, USA., Strub MP; Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Building 50, Bethesda, MD, 20892, USA., Taraska JW; Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Building 50, Bethesda, MD, 20892, USA. justin.taraska@nih.gov.

Publikováno v: Nature communications [Nat Commun] 2022 Feb 16; Vol. 13 (1), pp. 905. Date of Electronic Publication: 2022 Feb 16.

Sterols lower energetic barriers of membrane bending and fission necessary for efficient clathrin-mediated endocytosis.

Autor: Anderson RH; Sanford School of Medicine, University of South Dakota, Sioux Falls, SD 57105, USA; Cellular Therapies and Stem Cell Biology Group, Sanford Research, Sioux Falls, SD 57104, USA., Sochacki KA; Laboratory of Molecular Biophysics, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20814, USA., Vuppula H; Department of Chemistry and Biochemistry, South Dakota State University, Brookings, SD 57007, USA; BioSystems Networks and Translational Research Center, Brookings, SD 57007, USA., Scott BL; Nanoscience and Nanoengineering, South Dakota School of Mines & Technology, Rapid City, SD 57701, USA., Bailey EM; Department of Chemistry and Biochemistry, South Dakota State University, Brookings, SD 57007, USA; BioSystems Networks and Translational Research Center, Brookings, SD 57007, USA., Schultz MM; Cellular Therapies and Stem Cell Biology Group, Sanford Research, Sioux Falls, SD 57104, USA., Kerkvliet JG; Department of Chemistry and Biochemistry, South Dakota State University, Brookings, SD 57007, USA; BioSystems Networks and Translational Research Center, Brookings, SD 57007, USA., Taraska JW; Laboratory of Molecular Biophysics, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20814, USA., Hoppe AD; Department of Chemistry and Biochemistry, South Dakota State University, Brookings, SD 57007, USA; BioSystems Networks and Translational Research Center, Brookings, SD 57007, USA. Electronic address: adam.hoppe@sdstate.edu., Francis KR; Cellular Therapies and Stem Cell Biology Group, Sanford Research, Sioux Falls, SD 57104, USA; Department of Pediatrics, Sanford School of Medicine, University of South Dakota, Sioux Falls, SD 57105, USA. Electronic address: kevin.francis@sanfordhealth.org.

Publikováno v: Cell reports [Cell Rep] 2021 Nov 16; Vol. 37 (7), pp. 110008.