Por favor, use este identificador para citar o enlazar este Item:http://hdl.handle.net/20.500.12105/17653
Título
NIPBL and cohesin: new take on a classic tale.
Autor(es)
Alonso-Gil, Dácil | Losada, Ana CNIO
Fecha de publicación
2023-10
Cita
Trends Cell Biol . 2023;33(10):860-871.
Idioma
Inglés
Tipo de documento
journal article
Resumen
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).
MESH
Versión en línea
DOI
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- NIPBLandcohesin_2023.pdf
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