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  1. Article ; Online: Structural insights into the activation of ataxia-telangiectasia mutated by oxidative stress.

    Howes, Anna C / Perisic, Olga / Williams, Roger L

    Science advances

    2023  Volume 9, Issue 39, Page(s) eadi8291

    Abstract: Ataxia-telangiectasia mutated (ATM) is a master kinase regulating DNA damage response that is activated by DNA double-strand breaks. However, ATM is also directly activated by reactive oxygen species, but how oxidative activation is achieved remains ... ...

    Abstract Ataxia-telangiectasia mutated (ATM) is a master kinase regulating DNA damage response that is activated by DNA double-strand breaks. However, ATM is also directly activated by reactive oxygen species, but how oxidative activation is achieved remains unknown. We determined the cryo-EM structure of an H
    Language English
    Publishing date 2023-09-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.adi8291
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  2. Article ; Online: Structural Mechanisms of PTEN Regulation.

    Masson, Glenn R / Williams, Roger L

    Cold Spring Harbor perspectives in medicine

    2020  Volume 10, Issue 3

    Abstract: The tumor ... ...

    Abstract The tumor suppressor
    MeSH term(s) Amino Acid Sequence ; Humans ; Mutation ; Neoplasms/genetics ; Neoplasms/metabolism ; PTEN Phosphohydrolase/chemistry ; PTEN Phosphohydrolase/genetics ; PTEN Phosphohydrolase/metabolism ; Phosphorylation
    Chemical Substances PTEN Phosphohydrolase (EC 3.1.3.67) ; PTEN protein, human (EC 3.1.3.67)
    Language English
    Publishing date 2020-03-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 2157-1422
    ISSN (online) 2157-1422
    DOI 10.1101/cshperspect.a036152
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  3. Article ; Online: Prime Time for Dimeric Cytohesins: Surveying the Membrane with One Foot at a Time.

    Anandapadamanaban, Madhanagopal / Williams, Roger L

    Structure (London, England : 1993)

    2019  Volume 27, Issue 12, Page(s) 1739–1741

    Abstract: In this issue of Structure, Das et al. (2019) probe the structure and dynamics of dimeric cytohesins (guanine nucleotide exchange factors for ADP-ribosylation factors), in solution and on membranes. Unleashing an arsenal of methods, they demonstrate that ...

    Abstract In this issue of Structure, Das et al. (2019) probe the structure and dynamics of dimeric cytohesins (guanine nucleotide exchange factors for ADP-ribosylation factors), in solution and on membranes. Unleashing an arsenal of methods, they demonstrate that a pleckstrin-homology domain-mediated membrane recruitment promotes conformational changes that prime cytohesins for allosteric activation.
    MeSH term(s) ADP-Ribosylation Factors ; Guanine Nucleotide Exchange Factors ; Pleckstrin Homology Domains
    Chemical Substances Guanine Nucleotide Exchange Factors ; ADP-Ribosylation Factors (EC 3.6.5.2)
    Language English
    Publishing date 2019-12-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2019.11.009
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    Zs.A 4141: Show issues Location:
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  4. Article ; Online: Unsaturation, curvature and charge: effects of membrane parameters on PIK3C3/VPS34-containing complexes.

    Ohashi, Yohei / Tremel, Shirley / Williams, Roger L

    Autophagy

    2021  Volume 17, Issue 3, Page(s) 823–825

    Abstract: Phosphatidylinositol-3-phosphate (PtdIns3P) is essential for generating autophagosomes and regulating endocytic trafficking. Recently, we have shown that the activities of human PIK3C3/VPS34-containing complexes I and II, which synthesize PtdIns3P, are ... ...

    Abstract Phosphatidylinositol-3-phosphate (PtdIns3P) is essential for generating autophagosomes and regulating endocytic trafficking. Recently, we have shown that the activities of human PIK3C3/VPS34-containing complexes I and II, which synthesize PtdIns3P, are greatly affected by three membrane physicochemical parameters: lipid unsaturation, membrane curvature, and negative charge. Both complexes are more active on membranes composed of unsaturated lipids than saturated lipids, and high membrane curvature can compensate for the negative effect of high lipid saturation. Negatively charged phosphatidylserine (PS) activates the complexes, as well as PIK3C3/VPS34 alone. The kinase activity of complex I depends critically on the ATG14 BATS domain, whereas complex II relies on the BECN1 BARA domain. Our findings highlight the importance of the membrane character as sensed by the unique membrane binding motifs/domain of the complexes for regulating PIK3C3/VPS34 activity.
    MeSH term(s) Autophagosomes ; Autophagy ; Autophagy-Related Proteins ; Class III Phosphatidylinositol 3-Kinases ; Endosomes ; Humans
    Chemical Substances Autophagy-Related Proteins ; Class III Phosphatidylinositol 3-Kinases (EC 2.7.1.137)
    Language English
    Publishing date 2021-01-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2021.1872190
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    Zs.A 6741: Show issues Location:
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  5. Article ; Online: Ragtime Regulation: Mechanism of TORC1 Activation in Nutrient Sensing.

    Williams, Roger L / Anandapadamanaban, Madhanagopal

    Biochemistry

    2017  Volume 56, Issue 49, Page(s) 6411–6412

    MeSH term(s) Animals ; Enzyme Activation ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Nutritional Physiological Phenomena ; Protein Binding ; Saccharomyces cerevisiae/metabolism
    Chemical Substances Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1)
    Language English
    Publishing date 2017-11-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.7b01120
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    Zs.A 217: Show issues Location:
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  6. Article: Paradoxical dominant negative activity of an immunodeficiency-associated activating

    Tomlinson, Patsy R / Knox, Rachel / Perisic, Olga / Su, Helen C / Brierley, Gemma V / Williams, Roger L / Semple, Robert K

    bioRxiv : the preprint server for biology

    2023  

    Abstract: ... ...

    Abstract PIK3R1
    Language English
    Publishing date 2023-12-13
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.11.02.565250
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  7. Article ; Online: Dietary supplements and regulation.

    Williams, Roger L

    JAMA

    2011  Volume 306, Issue 15, Page(s) 1657; author reply 1657–8

    MeSH term(s) Dietary Supplements/classification ; Dietary Supplements/standards ; Humans ; Legislation as Topic ; Product Labeling ; United States Food and Drug Administration
    Language English
    Publishing date 2011-10-19
    Publishing country United States
    Document type Comment ; Letter
    ZDB-ID 2958-0
    ISSN 1538-3598 ; 0254-9077 ; 0002-9955 ; 0098-7484
    ISSN (online) 1538-3598
    ISSN 0254-9077 ; 0002-9955 ; 0098-7484
    DOI 10.1001/jama.2011.1494
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    Ua VI Zs.88: Show issues Location:
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  8. Article ; Online: Membrane trafficking: Arls squeeze the fat out.

    Williams, Roger L

    Nature chemical biology

    2011  Volume 7, Issue 12, Page(s) 863–864

    MeSH term(s) ADP-Ribosylation Factors/metabolism ; Animals ; Cyclic Nucleotide Phosphodiesterases, Type 6/metabolism ; GTP-Binding Proteins/metabolism ; Guanosine Triphosphate/metabolism ; Humans
    Chemical Substances Guanosine Triphosphate (86-01-1) ; Cyclic Nucleotide Phosphodiesterases, Type 6 (EC 3.1.4.35) ; ARL2 protein, human (EC 3.6.1.-) ; Arl2 protein, mouse (EC 3.6.1.-) ; GTP-Binding Proteins (EC 3.6.1.-) ; Arl3 protein, mouse (EC 3.6.1.2) ; ADP-Ribosylation Factors (EC 3.6.5.2) ; ARL3 protein, human (EC 3.6.5.2)
    Language English
    Publishing date 2011-11-15
    Publishing country United States
    Document type News ; Comment
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/nchembio.713
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    Zs.A 6251: Show issues Location:
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    Zs.MG 90: Show issues

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  9. Article ; Online: VPS34 complexes from a structural perspective.

    Ohashi, Yohei / Tremel, Shirley / Williams, Roger L

    Journal of lipid research

    2018  Volume 60, Issue 2, Page(s) 229–241

    Abstract: VPS34 phosphorylates phosphatidylinositol to produce PtdIns3P and is the progenitor of the phosphoinositide 3-kinase (PI3K) family. VPS34 has a simpler domain organization than class I PI3Ks, which belies the complexity of its quaternary organization, ... ...

    Abstract VPS34 phosphorylates phosphatidylinositol to produce PtdIns3P and is the progenitor of the phosphoinositide 3-kinase (PI3K) family. VPS34 has a simpler domain organization than class I PI3Ks, which belies the complexity of its quaternary organization, with the enzyme always functioning within larger assemblies. PtdIns3P recruits specific recognition modules that are common in protein-sorting pathways, such as autophagy and endocytic sorting. It is best characterized in two heterotetramers, complexes I and II. Complex I is composed of VPS34, VPS15, Beclin 1, and autophagy-related gene (ATG)14L, whereas complex II replaces ATG14L with UVRAG. Because VPS34 can form a component of several distinct complexes, it enables independent regulation of various pathways that are controlled by PtdIns3P. Complexes I and II are critical for early events in autophagy and endocytic sorting, respectively. Autophagy has a complex association with cancer. In early stages, it inhibits tumorigenesis, but in later stages, it acts as a survival factor for tumors. Recently, various disease-associated somatic mutations were found in genes encoding complex I and II subunits. Lipid kinase activities of the complexes are also influenced by posttranslational modifications (PTMs). Mapping PTMs and somatic mutations on three-dimensional models of the complexes suggests mechanisms for how these affect VPS34 activity.
    MeSH term(s) Class III Phosphatidylinositol 3-Kinases/antagonists & inhibitors ; Class III Phosphatidylinositol 3-Kinases/chemistry ; Class III Phosphatidylinositol 3-Kinases/genetics ; Class III Phosphatidylinositol 3-Kinases/metabolism ; Endocytosis ; Enzyme Inhibitors/pharmacology ; Humans ; Protein Processing, Post-Translational
    Chemical Substances Enzyme Inhibitors ; Class III Phosphatidylinositol 3-Kinases (EC 2.7.1.137)
    Language English
    Publishing date 2018-11-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 80154-9
    ISSN 1539-7262 ; 0022-2275
    ISSN (online) 1539-7262
    ISSN 0022-2275
    DOI 10.1194/jlr.R089490
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    Zs.A 175: Show issues Location:
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  10. Article: Synergy in activating class I PI3Ks.

    Burke, John E / Williams, Roger L

    Trends in biochemical sciences

    2015  Volume 40, Issue 2, Page(s) 88–100

    Abstract: The class I phosphoinositide 3-kinases (PI3Ks) are lipid kinases that transduce a host of cellular signals and regulate a broad range of essential functions including growth, proliferation, and migration. As such, PI3Ks have pivotal roles in diseases ... ...

    Abstract The class I phosphoinositide 3-kinases (PI3Ks) are lipid kinases that transduce a host of cellular signals and regulate a broad range of essential functions including growth, proliferation, and migration. As such, PI3Ks have pivotal roles in diseases such as cancer, diabetes, primary immune disorders, and inflammation. These enzymes are activated downstream of numerous activating stimuli including receptor tyrosine kinases, G protein-coupled receptors (GPCRs), and the Ras superfamily of small G proteins. A major challenge is to decipher how each PI3K isoform is able to successfully synergize these inputs into their intended signaling function. This article highlights recent progress in characterizing the molecular mechanisms of PI3K isoform-specific activation pathways, as well as novel roles for PI3Ks in human diseases, specifically cancer and immune diseases.
    MeSH term(s) Cell Movement/genetics ; Cell Proliferation/genetics ; Humans ; Immune System Diseases/enzymology ; Immune System Diseases/genetics ; Neoplasms/enzymology ; Neoplasms/genetics ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositols ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction
    Chemical Substances Phosphatidylinositols ; Protein Isoforms ; Receptors, G-Protein-Coupled ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
    Language English
    Publishing date 2015-01-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2014.12.003
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    Zs.A 1207: Show issues Location:
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