Transcription factor LSF facilitiates lysine methylation of α-tubulin by microtubule-associated SET8
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First author draft
Date
2019-06-10
DOI
Authors
Schaus, Scott
Hansen, Ulla
Chin, Hang Gyeong
Estève, Pierre Olivier
Ruse, Cristian
Lee, Jiyoung
Pradhan, Sriharsa
Version
First author draft
OA Version
Citation
Scott Schaus, Ulla Hansen, Hang Gyeong Chin, Pierre Olivier Estève, Cristian Ruse, Jiyoung Lee, Sriharsa Pradhan. "Transcription factor LSF facilitiates lysine methylation of α-tubulin by microtubule-associated SET8." https://doi.org/10.1101/665984
Abstract
Microtubules are critical for mitosis, cell motility, and protein and organelle transport, and are a validated target for anticancer drugs. However, tubulin regulation and recruitment in these cellular processes is less understood. Post-translational modifications of tubulin are proposed to regulate microtubule functions and dynamics. Although many such modifications have been investigated, tubulin methylations and enzymes responsible for methylation have only recently begun to be described. Here we report that N-lysine methyl transferase KMT5A (SET8/PR-Set7), which methylates histone H4K20, also methylates α-tubulin. Furthermore, the transcription factor LSF binds both tubulin and SET8, and enhances α-tubulin methylation in vitro, countered by FQI1, a specific small molecule inhibitor of LSF. Thus, the three proteins SET8, LSF, and tubulin, all essential for mitotic progression, interact with each other. Overall, these results point to dual functions for both SET8 and LSF not only in chromatin regulation, but also for cytoskeletal modification.
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The copyright holder for this preprint is the author/funder. It is made available under a CC-BY 4.0 International license.