2026-06-14T03:38:24Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/176532024-11-29T14:28:57Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597
Repisalud
author
Alonso-Gil, Dácil
author
Losada, Ana
funder
Ministerio de Ciencia e Innovación (España)
2024-02-08T17:04:27Z
2024-02-08T17:04:27Z
2023-10
Trends Cell Biol . 2023;33(10):860-871.
10.1016/j.tcb.2023.03.006
1879-3088
Trends in cell biology
37062615
http://hdl.handle.net/20.500.12105/17653
Cohesin folds the genome in dynamic chromatin loops and holds the sister chromatids together. NIPBLScc2 is currently considered the cohesin loader, a role that may need reevaluation. NIPBL activates the cohesin ATPase, which is required for topological entrapment of sister DNAs and to fuel DNA loop extrusion, but is not required for chromatin association. Mechanistic dissection of these processes suggests that both NIPBL and the cohesin STAG subunit bind DNA. NIPBL also regulates conformational switches of the complex. Interactions of NIPBL with chromatin factors, including remodelers, replication proteins, and the transcriptional machinery, affect cohesin loading and distribution. Here, we discuss recent research addressing how NIPBL modulates cohesin activities and how its mutation causes a developmental disorder, Cornelia de Lange Syndrome (CdLS).
eng
NIPBL and cohesin: new take on a classic tale.
journal article
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URL
https://repisalud.isciii.es/bitstreams/088189ec-274c-4b32-9c04-4f037e77e6cf/download
File
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application/pdf
NIPBLandcohesin_2023.pdf
URL
https://repisalud.isciii.es/bitstreams/1f767941-4aed-4975-af11-e666b272162f/download
File
MD5
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text/plain
NIPBLandcohesin_2023.pdf.txt