Hsp70 protects mitotic cells against heat-induced centrosome damage and division abnormalities

HMJ Hut, HH Kampinga, OCM Sibon*

*Corresponding author for this work

    Research output: Contribution to journalArticleAcademicpeer-review

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    Abstract

    The effect of heat shock on centrosomes has been mainly studied in interphase cells. Centrosomes play a key role in proper segregation of DNA during mitosis. However, the direct effect and consequences of heat shock on mitotic cells and a possible cellular defense system against proteotoxic stress during mitosis have not been described in detail. Here, we show that mild heat shock, applied during mitosis, causes loss of dynamitin/p5O antibody staining from centrosomes and kinetochores. In addition, it induces division errors in most cells and in the remaining cells progression through mitosis is delayed. Expression of heat shock protein (Hsp)70 protects against most heat-induced division abnormalities. On heat shock, Hsp70 is rapidly recruited to mitotic centrosomes and normal progression through mitosis is observed immediately after release of Hsp70 from centrosomes. In addition, Hsp70 expression coincides with restoration of dynamitin/p50 antibody staining at centrosomes but not at kinetochores. Our data show that during mitosis, centrosomes are particularly affected resulting in abnormal mitosis. Hsp70 is sufficient to protect against most division abnormalities, demonstrating the involvement of Hsp70 in a repair mechanism of heat-damaged mitotic centrosomes.

    Original languageEnglish
    Pages (from-to)3776-3785
    Number of pages10
    JournalMolecular Biology of the Cell
    Volume16
    Issue number8
    DOIs
    Publication statusPublished - Aug-2005

    Keywords

    • HAMSTER OVARY CELLS
    • MOLECULAR CHAPERONES
    • CYCLE PROGRESSION
    • SHOCK PROTEINS
    • HELA-CELLS
    • S-PHASE
    • KINETOCHORE
    • MITOSIS
    • THERMOTOLERANCE
    • ORGANIZATION

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