2026-04-29T06:15:42Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/164662024-09-27T09:14:06Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605
Repisalud
author
Campos-Iglesias, Diana
author
Fraile, Julia M
author
Bretones, Gabriel
author
Montero, Alejandro A
author
Bonzon-Kulichenko, Elena
author
Vazquez, Jesus
author
López-Otín, Carlos
author
Freije, José M P
funder
Ministerio de Ciencia e Innovación (España)
funder
Fundación La Caixa
funder
Unión Europea. Comisión Europea. European Research Council (ERC)
funder
Fundación Cajastur-Liberbank
2023-09-15T09:22:06Z
2023-09-15T09:22:06Z
2023-01-26
Cell Death Dis. 2023 Jan 26;14(1):60.
http://hdl.handle.net/20.500.12105/16466
36702832
10.1038/s41419-023-05600-x
2041-4889
Cell death & disease
The spindle assembly checkpoint (SAC) is an essential mechanism that ensures the accurate chromosome segregation during mitosis, thus preventing genomic instability. Deubiquitinases have emerged as key regulators of the SAC, mainly by determining the fate of proteins during cell cycle progression. Here, we identify USP49 deubiquitinase as a novel regulator of the spindle checkpoint. We show that loss of USP49 in different cancer cell lines impairs proliferation and increases aneuploidy. In addition, USP49-depleted cells overcome the arrest induced by the SAC in the presence of nocodazole. Finally, we report new binding partners of USP49, including ribophorin 1, USP44, and different centrins.
eng
USP49 deubiquitinase regulates the mitotic spindle checkpoint and prevents aneuploidy.
journal article
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USP49 deubiquitinase regulates_Cell Death Dis_2023.pdf
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https://repisalud.isciii.es/bitstreams/720034b3-60b0-4413-bdde-0b94c8f63002/download
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10f7713b9ee731fbd820eae412cefcff
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USP49 deubiquitinase regulates_Cell Death Dis_2023.pdf.txt