We have updated our privacy policy. If you have any question, contact us at privacy@scicrunch.org. Dismiss and don't show again

Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

TRIM24 links a non-canonical histone signature to breast cancer.

Nature | Dec 16, 2010

Recognition of modified histone species by distinct structural domains within 'reader' proteins plays a critical role in the regulation of gene expression. Readers that simultaneously recognize histones with multiple marks allow transduction of complex chromatin modification patterns into specific biological outcomes. Here we report that chromatin regulator tripartite motif-containing 24 (TRIM24) functions in humans as a reader of dual histone marks by means of tandem plant homeodomain (PHD) and bromodomain (Bromo) regions. The three-dimensional structure of the PHD-Bromo region of TRIM24 revealed a single functional unit for combinatorial recognition of unmodified H3K4 (that is, histone H3 unmodified at lysine 4, H3K4me0) and acetylated H3K23 (histone H3 acetylated at lysine 23, H3K23ac) within the same histone tail. TRIM24 binds chromatin and oestrogen receptor to activate oestrogen-dependent genes associated with cellular proliferation and tumour development. Aberrant expression of TRIM24 negatively correlates with survival of breast cancer patients. The PHD-Bromo of TRIM24 provides a structural rationale for chromatin activation through a non-canonical histone signature, establishing a new route by which chromatin readers may influence cancer pathogenesis.

Pubmed ID: 21164480 RIS Download

Mesh terms: Acetylation | Breast Neoplasms | Carrier Proteins | Cell Line, Tumor | Chromatin | Chromatin Assembly and Disassembly | Crystallography, X-Ray | Estrogen Receptor alpha | Estrogens | Gene Expression Regulation, Neoplastic | HEK293 Cells | Histones | Humans | Methylation | Protein Array Analysis | Protein Binding | Protein Structure, Tertiary | Substrate Specificity | Survival Rate

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

Associated grants

  • Agency: NIDDK NIH HHS, Id: P30DK078392-01
  • Agency: NICHD NIH HHS, Id: T32 HD07325
  • Agency: NIGMS NIH HHS, Id: GM081627
  • Agency: NIDDK NIH HHS, Id: P30 DK078392
  • Agency: NICHD NIH HHS, Id: T32 HD007325
  • Agency: NIGMS NIH HHS, Id: P01 GM081627
  • Agency: NIGMS NIH HHS, Id: P01 GM081627-010003
  • Agency: NIBIB NIH HHS, Id: P30 EB009998
  • Agency: NIGMS NIH HHS, Id: R01 GM079641
  • Agency: NIGMS NIH HHS, Id: P01 GM081627-020003
  • Agency: NIGMS NIH HHS, Id: GM079641
  • Agency: NCATS NIH HHS, Id: UL1 TR000077
  • Agency: NCRR NIH HHS, Id: U54 RR025216

BioGRID (Data, Interactions)

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.