Comparative interactomes of HSF1 in stress and disease reveal a role for CTCF in HSF1-mediated gene regulation

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dc.contributor.author Burchfiel, Eileen T.
dc.contributor.author Vihervaara, Anniina
dc.contributor.author Guertin, Michael J.
dc.contributor.author Gomez-Pastor, Rocio
dc.contributor.author Thiele, Dennis J.
dc.date.accessioned 2022-03-04T15:21:03Z
dc.date.available 2022-03-04T15:21:03Z
dc.date.issued 2021
dc.identifier.citation Burchfiel , E T , Vihervaara , A , Guertin , M J , Gomez-Pastor , R & Thiele , D J 2021 , ' Comparative interactomes of HSF1 in stress and disease reveal a role for CTCF in HSF1-mediated gene regulation ' , Journal of Biological Chemistry , vol. 296 , 100097 . https://doi.org/10.1074/jbc.RA120.015452
dc.identifier.other PURE: 175022701
dc.identifier.other PURE UUID: b9ea7bd4-b256-4a20-9735-02eb909d8e2f
dc.identifier.other WOS: 000672866400077
dc.identifier.other Scopus: 85102841077
dc.identifier.other PubMed: 33208463
dc.identifier.uri http://hdl.handle.net/10138/341310
dc.description.abstract Heat shock transcription factor 1 (HSF1) orchestrates cellular stress protection by activating or repressing gene transcription in response to protein misfolding, oncogenic cell proliferation, and other environmental stresses. HSF1 is tightly regulated via intramolecular repressive interactions, post-ranslational modifications, and protein-protein interactions. How these HSF1 regulatory protein interactions are altered in response to acute and chronic stress is largely unknown. To elucidate the profile of HSF1 protein interactions under normal growth and chronic and acutely stressful conditions, quantitative proteomics studies identified interacting proteins in the response to heat shock or in the presence of a poly-glutamine aggregation protein cell-based model of Huntington's disease. These studies identified distinct protein interaction partners of HSF1 as well as changes in the magnitude of shared interactions as a function of each stressful condition. Several novel HSF1-interacting proteins were identified that encompass a wide variety of cellular functions, including roles in DNA repair, mRNA processing, and regulation of RNA polymerase II. One HSF1 partner, CTCF, interacted with HSF1 in a stress-inducible manner and functions in repression of specific HSF1 target genes. Understanding how HSF1 regulates gene repression is a crucial question, given the dysregulation of HSF1 target genes in both cancer and neurodegeneration. These studies expand our understanding of HSF1-mediated gene repression and provide key insights into HSF1 regulation via protein-protein interactions. en
dc.format.extent 18
dc.language.iso eng
dc.relation.ispartof Journal of Biological Chemistry
dc.rights cc_by
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject 1182 Biochemistry, cell and molecular biology
dc.title Comparative interactomes of HSF1 in stress and disease reveal a role for CTCF in HSF1-mediated gene regulation en
dc.type Article
dc.contributor.organization Institute of Biotechnology
dc.description.reviewstatus Peer reviewed
dc.relation.doi https://doi.org/10.1074/jbc.RA120.015452
dc.relation.issn 0021-9258
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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