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Heat shock-induced mitotic arrest requires heat shock protein 105 for the activation of spindle assembly checkpoint.

07:00 EST 29th November 2018 | BioPortfolio

Summary of "Heat shock-induced mitotic arrest requires heat shock protein 105 for the activation of spindle assembly checkpoint."

Heat shock causes proteotoxic stress that induces various cellular responses, including delayed mitotic progression and the generation of an aberrant number of chromosomes. In this study, heat shock delayed the onset of anaphase by increasing the number of misoriented cells, accompanied by the kinetochore localization of budding uninhibited by benzimidazole-related (BubR)1 in a monopolar spindle (Mps)1-dependent manner. The mitotic delay was canceled by knockdown of mitotic arrest defect (Mad)2. Knockdown of heat shock protein (Hsp)105 partially abrogated the mitotic delay with the loss of the kinetochore localization of BubR1 under heat shock conditions and accelerated mitotic progression under nonstressed conditions. Consistent with this result, Hsp105 knockdown increased the number of anaphase cells with lagging chromosomes, through mitotic slippage, and decreased taxol sensitivity more than Mad2 knockdown. Hsp105 was coprecipitated with cell division cycle (Cdc)20 in an Mps1-dependent manner; however, its knockdown did not affect coprecipitation of Mad2 and BubR1 with Cdc20. We propose that heat shock delays the onset of anaphase via the activation of the spindle assembly checkpoint (SAC). Hsp105 prevents abnormal cell division by contributing to SAC activation under heat shock and nonstressed conditions by interacting with Cdc20 but not affecting formation of the mitotic checkpoint complex.-Kakihana, A., Oto, Y., Saito, Y., Nakayama, Y. Heat shock-induced mitotic arrest requires heat shock protein 105 for the activation of spindle assembly checkpoint.

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This article was published in the following journal.

Name: FASEB journal : official publication of the Federation of American Societies for Experimental Biology
ISSN: 1530-6860
Pages: fj201801369R

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Medical and Biotech [MESH] Definitions

A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.

Heat and cold stress-inducible, transcription factors that bind to inverted 5'-NGAAN-3' pentamer DNA sequences and are regulated by poly(ADP) ribosylation. They play essential roles as transcriptional activators of the HEAT-SHOCK RESPONSE by inducing expression of large classes of MOLECULAR CHAPERONES and heat-shock proteins. They also function in DNA REPAIR; transcriptional reactivation of latent HIV-1; and pre-mRNA processing and nuclear export of HSP70 HEAT-SHOCK PROTEINS during heat stress.

A subfamily of small heat-shock proteins that are closely related to ALPHA B-CRYSTALLIN. Hsp20 heat-shock proteins can undergo PHOSPHORYLATION by CYCLIC GMP-DEPENDENT PROTEIN KINASES.

Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.

A group of eukaryotic high-molecular mass heat-shock proteins that represent a subfamily of HSP70 HEAT-SHOCK PROTEINS. Hsp110 proteins prevent protein aggregation and can maintain denatured proteins in folding-competent states.

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