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    Endoplasmic reticulum chaperone Gp96 controls actomyosin dynamics and protects against pore-forming toxins

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    Blagg_2016.pdf (3.412Mb)
    Issue Date
    2016-02-12
    Author
    Ghosh, Suman
    Shinogle, Heather E.
    Galeva, Nadezhda A.
    Dobrowsky, Rick T.
    Blagg, Brian S. J.
    Publisher
    American Society for Biochemistry and Molecular Biology
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
    Rights
    © The American Society for Biochemistry and Molecular Biology.
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    Abstract
    Heat shock protein 90 (HSP90) is a molecular chaperone that is up-regulated in cancer and is required for the folding of numerous signaling proteins. Consequently, HSP90 represents an ideal target for the development of new anti-cancer agents. The human HSP90 isoform, glucose-regulated protein 94 (GRP94), resides in the endoplasmic reticulum and regulates secretory pathways, integrins, and Toll-like receptors, which contribute to regulating immunity and metastasis. However, the cellular function of GRP94 remains underinvestigated. We report that GRP94 knockdown cells are defective in intracellular transport and, consequently, negatively impact the trafficking of F-actin toward the cellular cortex, integrin α2 and integrin αL toward the cell membrane and filopodia, and secretory vesicles containing the HSP90α-AHA1-survivin complex toward the leading edge. As a result, GRP94 knockdown cells form a multipolar spindle instead of bipolar morphology and consequently manifest a defect in cell migration and adhesion.
    Description
    This research was originally published in the Journal of Biological Chemistry. Suman Ghosh, Heather E. Shinogle, Nadezhda A. Galeva, Rick T. Dobrowsky, and Brian S. J. Blagg. Endoplasmic Reticulum-resident Heat Shock Protein 90 (HSP90) Isoform Glucose-regulated Protein 94 (GRP94) Regulates Cell Polarity and Cancer Cell Migration by Affecting Intracellular Transport. Journal of Biological Chemistry. 2016; 291, 8309-8323.
    URI
    http://hdl.handle.net/1808/25243
    DOI
    https://doi.org/10.1074/jbc.M115.688374
    Collections
    • Medicinal Chemistry Scholarly Works [244]
    Citation
    Ghosh, S., Shinogle, H. E., Galeva, N. A., Dobrowsky, R. T., & Blagg, B. S. (2016). Endoplasmic reticulum-resident heat shock protein 90 (HSP90) isoform glucose-regulated protein 94 (GRP94) regulates cell polarity and cancer cell migration by affecting intracellular transport. Journal of Biological Chemistry, 291(16), 8309-8323.

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    KU Libraries
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    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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