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EZH2 noncanonically binds cMyc and p300 through a cryptic transactivation domain to mediate gene act...

EZH2 noncanonically binds cMyc and p300 through a cryptic transactivation domain to mediate gene act...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2639130477

EZH2 noncanonically binds cMyc and p300 through a cryptic transactivation domain to mediate gene activation and promote oncogenesis

About this item

Full title

EZH2 noncanonically binds cMyc and p300 through a cryptic transactivation domain to mediate gene activation and promote oncogenesis

Publisher

London: Nature Publishing Group UK

Journal title

Nature cell biology, 2022-03, Vol.24 (3), p.384-399

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Canonically, EZH2 serves as the catalytic subunit of PRC2, which mediates H3K27me3 deposition and transcriptional repression. Here, we report that in acute leukaemias, EZH2 has additional noncanonical functions by binding cMyc at non-PRC2 targets and uses a hidden transactivation domain (TAD) for (co)activator recruitment and gene activation. Both...

Alternative Titles

Full title

EZH2 noncanonically binds cMyc and p300 through a cryptic transactivation domain to mediate gene activation and promote oncogenesis

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2639130477

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2639130477

Other Identifiers

ISSN

1465-7392

E-ISSN

1476-4679

DOI

10.1038/s41556-022-00850-x

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