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An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.

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Title: An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.
Authors: Soubias O; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.; Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA., Foley SL; Department of Biophysics, The Johns Hopkins University, Baltimore, MD, USA., Jian X; Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA., Jackson RA; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA., Zhang Y; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.; Ring Therapeutics, Inc., Cambridge, MA, USA., Rosenberg EM Jr; Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA., Hu BJ; Unit of Membrane Chemical Physics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA., Li J; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA., Heinrich F; Department of Physics Carnegie Mellon University, Pittsburgh, PA, USA.; NIST Center for Neutron Research, Gaithersburg, MD, USA., Johnson ME; Department of Biophysics, The Johns Hopkins University, Baltimore, MD, USA., Sodt AJ; Unit of Membrane Chemical Physics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA., Randazzo PA; Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA. randazzp@mail.nih.gov., Byrd RA; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA. byrdra@nih.gov.
Source: Nature communications [Nat Commun] 2025 Sep 30; Vol. 16 (1), pp. 8701. Date of Electronic Publication: 2025 Sep 30.
Publication Type: Journal Article
Journal Info: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.
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  Data: <searchLink fieldCode="AU" term="%22Soubias+O%22">Soubias O</searchLink>; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.; Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.<br /><searchLink fieldCode="AU" term="%22Foley+SL%22">Foley SL</searchLink>; Department of Biophysics, The Johns Hopkins University, Baltimore, MD, USA.<br /><searchLink fieldCode="AU" term="%22Jian+X%22">Jian X</searchLink>; Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.<br /><searchLink fieldCode="AU" term="%22Jackson+RA%22">Jackson RA</searchLink>; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.<br /><searchLink fieldCode="AU" term="%22Zhang+Y%22">Zhang Y</searchLink>; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.; Ring Therapeutics, Inc., Cambridge, MA, USA.<br /><searchLink fieldCode="AU" term="%22Rosenberg+EM+Jr%22">Rosenberg EM Jr</searchLink>; Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.<br /><searchLink fieldCode="AU" term="%22Hu+BJ%22">Hu BJ</searchLink>; Unit of Membrane Chemical Physics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.<br /><searchLink fieldCode="AU" term="%22Li+J%22">Li J</searchLink>; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.<br /><searchLink fieldCode="AU" term="%22Heinrich+F%22">Heinrich F</searchLink>; Department of Physics Carnegie Mellon University, Pittsburgh, PA, USA.; NIST Center for Neutron Research, Gaithersburg, MD, USA.<br /><searchLink fieldCode="AU" term="%22Johnson+ME%22">Johnson ME</searchLink>; Department of Biophysics, The Johns Hopkins University, Baltimore, MD, USA.<br /><searchLink fieldCode="AU" term="%22Sodt+AJ%22">Sodt AJ</searchLink>; Unit of Membrane Chemical Physics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.<br /><searchLink fieldCode="AU" term="%22Randazzo+PA%22">Randazzo PA</searchLink>; Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA. randazzp@mail.nih.gov.<br /><searchLink fieldCode="AU" term="%22Byrd+RA%22">Byrd RA</searchLink>; Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA. byrdra@nih.gov.
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