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    Insulin Induces Microtubule Stabilization and Regulates the Microtubule Plus-end Tracking Protein Network in Adipocytes

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    Parker_et_al_Article.pdf
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    Final Accepted Manuscript
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    Author
    Parker, Sara S
    Krantz, James
    Kwak, Eun-A
    Barker, Natalie K
    Deer, Chris G
    Lee, Nam Y
    Mouneimne, Ghassan
    Langlais, Paul R
    Affiliation
    Univ Arizona, Coll Med, Dept Cellular & Mol Med
    Univ Arizona, Coll Med, Dept Med, Div Endocrinol
    Univ Arizona, Coll Med, Dept Pharmacol
    Univ Arizona, Coll Med, Dept Chem & Biochem
    Univ Arizona, Res Comp
    Issue Date
    2019-07
    Keywords
    Affinity proteomics
    CLASP2
    G2L1
    Insulin
    Interactome
    Label-free quantification
    Microtubules
    Phosphorylation
    Protein-Protein Interactions*
    Quantification
    
    Metadata
    Show full item record
    Publisher
    AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
    Citation
    Parker, S. S., Krantz, J., Kwak, E. A., Barker, N. K., Deer, C. G., Lee, N. Y., ... & Langlais, P. R. (2019). Insulin Induces Microtubule Stabilization and Regulates the Microtubule Plus-End Tracking Protein Network in Adipocytes. Molecular & Cellular Proteomics, mcp-RA119.
    Journal
    MOLECULAR & CELLULAR PROTEOMICS
    Rights
    © 2019 Parker et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    Insulin-stimulated glucose uptake is known to involve microtubules, although the function of microtubules and the microtubule-regulating proteins involved in insulin action are poorly understood. CLASP2, a plus-end tracking microtubule-associated protein (+TIP) that controls microtubule dynamics, was recently implicated as the first +TIP associated with insulin-regulated glucose uptake. Here, using protein-specific targeted quantitative phosphoproteomics within 3T3-L1 adipocytes, we discovered that insulin regulates phosphorylation of the CLASP2 network members G2L1, MARK2, CLIP2, AGAP3, and CKAP5 as well as EB1, revealing the existence of a previously unknown microtubule-associated protein system that responds to insulin. To further investigate, G2L1 interactome studies within 3T3-L1 adipocytes revealed that G2L1 coimmunoprecipitates CLASP2 and CLIP2 as well as the master integrators of +TIP assembly, the end binding (EB) proteins. Live-cell total internal reflection fluorescence microscopy in adipocytes revealed G2L1 and CLASP2 colocalize on microtubule plus-ends. We found that although insulin increases the number of CLASP2-containing plus-ends, insulin treatment simultaneously decreases CLASP2-containing plus-end velocity. In addition, we discovered that insulin stimulates redistribution of CLASP2 and G2L1 from exclusive plus-end tracking to "trailing" behind the growing tip of the microtubule. Insulin treatment increases alpha-tubulin Lysine 40 acetylation, a mechanism that was observed to be regulated by a counterbalance between GSK3 and mTOR, and led to microtubule stabilization. Our studies introduce insulin-stimulated microtubule stabilization and plus-end trailing of +TIPs as new modes of insulin action and reveal the likelihood that a network of microtubule-associated proteins synergize to coordinate insulin-regulated microtubule dynamics.
    ISSN
    1535-9476
    PubMed ID
    31018989
    DOI
    10.1074/mcp.RA119.001450
    Version
    Final accepted manuscript
    Sponsors
    TRIF Space Exploration and Optical Sciences (TRIF-SEOS) grant
    ae974a485f413a2113503eed53cd6c53
    10.1074/mcp.RA119.001450
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