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Title: Critical role for cold shock protein YB-1 in cytokinesis
Authors: Mehta, Sunali
Algie, Michael
Al-Jabry, Tariq
McKinney, Cushla
Kannan, Srinivasaraghavan
Verma, Chandra Shekhar
Ma, Weini
Zhang, Jessie
Bartolec, Tara K.
Masamsetti, V. Pragathi
Parker, Kim
Henderson, Luke
Gould, Maree L.
Bhatia, Puja
Harfoot, Rhodri
Chircop, Megan
Kleffmann, Torsten
Cohen, Scott B.
Woolley, Adele G.
Cesare, Anthony J.
Braithwaite, Antony
Keywords: Science::Biological sciences
Issue Date: 2020
Source: Mehta, S., Algie, M., Al-Jabri, T., McKinney, C., Kannan, S., Verma, C. S., . . . Braithwaite, A. (2020). Critical role for cold shock protein YB-1 in cytokinesis. Cancers, 12(9), 2473-. doi:10.1101/2020.03.18.997817
Journal: Cancers
Abstract: High levels of the cold shock protein Y-box-binding protein-1, YB-1, are tightly correlated with increased cell proliferation and progression. However, the precise mechanism by which YB-1 regulates proliferation is unknown. Here, we found that YB-1 depletion in several cancer cell lines and in immortalized fibroblasts resulted in cytokinesis failure and consequent multinucleation. Rescue experiments indicated that YB-1 was required for completion of cytokinesis. Using confocal imaging we found that YB-1 was essential for orchestrating the spatio-temporal distribution of the microtubules, β-actin and the chromosome passenger complex (CPC) to define the cleavage plane. We show that phosphorylation at six serine residues was essential for cytokinesis, of which novel sites were identified using mass spectrometry. Using atomistic modelling we show how phosphorylation at multiple sites alters YB-1 conformation, allowing it to interact with protein partners. Our results establish phosphorylated YB-1 as a critical regulator of cytokinesis, defining precisely how YB-1 regulates cell division.
ISSN: 2072-6694
DOI: 10.3390/cancers12092473
Rights: © 2020 The Authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (
Fulltext Permission: open
Fulltext Availability: With Fulltext
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