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    Phosphorylation controls autoinhibition of cytoplasmic linker protein-170

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    Article (3.733Mb)
    Supplementary materials (1.499Mb)
    Date
    2010-06-02
    Author
    Lee, Ho-Sup  Concept link
    Komarova, Yulia A.  Concept link
    Nadezhdina, Elena S.  Concept link
    Anjum, Rana  Concept link
    Peloquin, John G.  Concept link
    Schober, Joseph M.  Concept link
    Danciu, Oana  Concept link
    van Haren, Jeffrey  Concept link
    Galjart, Niels  Concept link
    Gygi, Steven P.  Concept link
    Akhmanova, Anna  Concept link
    Borisy, Gary G.  Concept link
    Metadata
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    Citable URI
    https://hdl.handle.net/1912/3840
    As published
    https://doi.org/10.1091/mbc.E09-12-1036
    DOI
    10.1091/mbc.E09-12-1036
    Abstract
    Cytoplasmic linker protein (CLIP)-170 is a microtubule (MT) plus-end-tracking protein that regulates MT dynamics and links MT plus ends to different intracellular structures. We have shown previously that intramolecular association between the N and C termini results in autoinhibition of CLIP-170, thus altering its binding to MTs and the dynactin subunit p150Glued (J. Cell Biol. 2004: 166, 1003–1014). In this study, we demonstrate that conformational changes in CLIP-170 are regulated by phosphorylation that enhances the affinity between the N- and C-terminal domains. By using site-directed mutagenesis and phosphoproteomic analysis, we mapped the phosphorylation sites in the third serine-rich region of CLIP-170. A phosphorylation-deficient mutant of CLIP-170 displays an "open" conformation and a higher binding affinity for growing MT ends and p150Glued as compared with nonmutated protein, whereas a phosphomimetic mutant confined to the "folded back" conformation shows decreased MT association and does not interact with p150Glued. We conclude that phosphorylation regulates CLIP-170 conformational changes resulting in its autoinhibition.
    Description
    Author Posting. © American Society for Cell Biology, 2010. This article is posted here by permission of American Society for Cell Biology for personal use, not for redistribution. The definitive version was published in Molecular Biology of the Cell 21 (2010): 2661-2673, doi:10.1091/mbc.E09-12-1036.
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    • Cellular Dynamics Program
    Suggested Citation
    Molecular Biology of the Cell 21 (2010): 2661-2673
     
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