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The Putative RNA-Binding Protein Dri1 Promotes the Loading of Kinesin-14/Klp2 to the Mitotic Spindle and Is Sequestered into Heat-Induced Protein Aggregates in Fission Yeast

1
Laboratory of Molecular and Chemical Cell Biology, Graduate School of Integrated Sciences for Life, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-8530, Japan
2
Hiroshima Research Center for Healthy Aging (HiHA), Hiroshima University, Hiroshima 739-8530, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: Leah Gheber
Int. J. Mol. Sci. 2021, 22(9), 4795; https://doi.org/10.3390/ijms22094795
Received: 15 March 2021 / Revised: 21 April 2021 / Accepted: 29 April 2021 / Published: 30 April 2021
(This article belongs to the Special Issue Cytoskeletal Dynamics and Regulation of Cell Cycle Progression)
Cells form a bipolar spindle during mitosis to ensure accurate chromosome segregation. Proper spindle architecture is established by a set of kinesin motors and microtubule-associated proteins. In most eukaryotes, kinesin-5 motors are essential for this process, and genetic or chemical inhibition of their activity leads to the emergence of monopolar spindles and cell death. However, these deficiencies can be rescued by simultaneous inactivation of kinesin-14 motors, as they counteract kinesin-5. We conducted detailed genetic analyses in fission yeast to understand the mechanisms driving spindle assembly in the absence of kinesin-5. Here, we show that deletion of the dri1 gene, which encodes a putative RNA-binding protein, can rescue temperature sensitivity caused by cut7-22, a fission yeast kinesin-5 mutant. Interestingly, kinesin-14/Klp2 levels on the spindles in the cut7 mutants were significantly reduced by the dri1 deletion, although the total levels of Klp2 and the stability of spindle microtubules remained unaffected. Moreover, RNA-binding motifs of Dri1 are essential for its cytoplasmic localization and function. We have also found that a portion of Dri1 is spatially and functionally sequestered by chaperone-based protein aggregates upon mild heat stress and limits cell division at high temperatures. We propose that Dri1 might be involved in post-transcriptional regulation through its RNA-binding ability to promote the loading of Klp2 on the spindle microtubules. View Full-Text
Keywords: fission yeast; kinesin-14; RNA-binding protein; mitotic spindle; heat stress fission yeast; kinesin-14; RNA-binding protein; mitotic spindle; heat stress
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MDPI and ACS Style

Yukawa, M.; Ohishi, M.; Yamada, Y.; Toda, T. The Putative RNA-Binding Protein Dri1 Promotes the Loading of Kinesin-14/Klp2 to the Mitotic Spindle and Is Sequestered into Heat-Induced Protein Aggregates in Fission Yeast. Int. J. Mol. Sci. 2021, 22, 4795. https://doi.org/10.3390/ijms22094795

AMA Style

Yukawa M, Ohishi M, Yamada Y, Toda T. The Putative RNA-Binding Protein Dri1 Promotes the Loading of Kinesin-14/Klp2 to the Mitotic Spindle and Is Sequestered into Heat-Induced Protein Aggregates in Fission Yeast. International Journal of Molecular Sciences. 2021; 22(9):4795. https://doi.org/10.3390/ijms22094795

Chicago/Turabian Style

Yukawa, Masashi, Mitsuki Ohishi, Yusuke Yamada, and Takashi Toda. 2021. "The Putative RNA-Binding Protein Dri1 Promotes the Loading of Kinesin-14/Klp2 to the Mitotic Spindle and Is Sequestered into Heat-Induced Protein Aggregates in Fission Yeast" International Journal of Molecular Sciences 22, no. 9: 4795. https://doi.org/10.3390/ijms22094795

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