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    Structural basis for membrane recruitment and allosteric activation of cytohesin family Arf GTPase exchange factors

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    Authors
    Malaby, Andrew W.
    van den Berg, Bert
    Lambright, David G.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    2013-08-27
    Keywords
    ADP-Ribosylation Factors
    Allosteric Site
    Catalytic Domain
    GTP Phosphohydrolases
    Models, Molecular
    Protein Conformation
    Surface Plasmon Resonance
    Biochemistry
    
    Metadata
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    Link to Full Text
    http://dx.doi.org/10.1073/pnas.1301883110
    Abstract
    Membrane recruitment of cytohesin family Arf guanine nucleotide exchange factors depends on interactions with phosphoinositides and active Arf GTPases that, in turn, relieve autoinhibition of the catalytic Sec7 domain through an unknown structural mechanism. Here, we show that Arf6-GTP relieves autoinhibition by binding to an allosteric site that includes the autoinhibitory elements in addition to the PH domain. The crystal structure of a cytohesin-3 construct encompassing the allosteric site in complex with the head group of phosphatidyl inositol 3,4,5-trisphosphate and N-terminally truncated Arf6-GTP reveals a large conformational rearrangement, whereby autoinhibition can be relieved by competitive sequestration of the autoinhibitory elements in grooves at the Arf6/PH domain interface. Disposition of the known membrane targeting determinants on a common surface is compatible with multivalent membrane docking and subsequent activation of Arf substrates, suggesting a plausible model through which membrane recruitment and allosteric activation could be structurally integrated.
    Source
    Malaby AW, van den Berg B, Lambright DG. Structural basis for membrane recruitment and allosteric activation of cytohesin family Arf GTPase exchange factors. Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14213-8. doi:10.1073/pnas.1301883110. Link to article on publisher's site
    DOI
    10.1073/pnas.1301883110
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/44406
    PubMed ID
    23940353
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1073/pnas.1301883110
    Scopus Count
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    UMass Chan Faculty and Researcher Publications

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