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TitleInteractome Rewiring Following Pharmacological Targeting of BET Bromodomains.
Journal, issue, pagesMol Cell, Vol. 73, Issue 3, Page 621-638.e17, Year 2019
Publish dateFeb 7, 2019
AuthorsJean-Philippe Lambert / Sarah Picaud / Takao Fujisawa / Huayun Hou / Pavel Savitsky / Liis Uusküla-Reimand / Gagan D Gupta / Hala Abdouni / Zhen-Yuan Lin / Monika Tucholska / James D R Knight / Beatriz Gonzalez-Badillo / Nicole St-Denis / Joseph A Newman / Manuel Stucki / Laurence Pelletier / Nuno Bandeira / Michael D Wilson / Panagis Filippakopoulos / Anne-Claude Gingras /
PubMed AbstractTargeting bromodomains (BRDs) of the bromo-and-extra-terminal (BET) family offers opportunities for therapeutic intervention in cancer and other diseases. Here, we profile the interactomes of BRD2, ...Targeting bromodomains (BRDs) of the bromo-and-extra-terminal (BET) family offers opportunities for therapeutic intervention in cancer and other diseases. Here, we profile the interactomes of BRD2, BRD3, BRD4, and BRDT following treatment with the pan-BET BRD inhibitor JQ1, revealing broad rewiring of the interaction landscape, with three distinct classes of behavior for the 603 unique interactors identified. A group of proteins associate in a JQ1-sensitive manner with BET BRDs through canonical and new binding modes, while two classes of extra-terminal (ET)-domain binding motifs mediate acetylation-independent interactions. Last, we identify an unexpected increase in several interactions following JQ1 treatment that define negative functions for BRD3 in the regulation of rRNA synthesis and potentially RNAPII-dependent gene expression that result in decreased cell proliferation. Together, our data highlight the contributions of BET protein modules to their interactomes allowing for a better understanding of pharmacological rewiring in response to JQ1.
External linksMol Cell / PubMed:30554943 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution1.15 - 2.22 Å
Structure data

SASDCR2:
Bromodomain-containing protein 4 (BRD4) tandem bromodomains
Method: SAXS/SANS

SASDCS2:
Bromodomain-containing protein 3 (BRD3) tandem bromodomains
Method: SAXS/SANS

SASDCT2:
Bromodomain-containing protein 2 (BRD2) tandem bromodomains
Method: SAXS/SANS

SASDCU2:
Bromodomain testis-specific protein (BRDT) tandem bromodomains
Method: SAXS/SANS

PDB-5nnc:
Crystal Structure of the first bromodomain of human BRD4 in complex with a diacetylated histone 4 peptide (H3K9ac/K14ac)
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

PDB-5nnd:
Crystal Structure of the first bromodomain of human BRD4 in complex with a diacetylated histone 4 peptide (H3K9ac/K14ac)
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

PDB-5nne:
Crystal Structure of the first bromodomain of human BRD4 in complex with a diacetylated TOP2A peptide (K1201ac/K1204ac)
Method: X-RAY DIFFRACTION / Resolution: 1.15 Å

PDB-5nnf:
Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated BAZ1B peptide (K221ac)
Method: X-RAY DIFFRACTION / Resolution: 1.15 Å

PDB-5nng:
Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated SRPK1 peptide (K585ac)
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-6g0o:
Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated ATRX peptide (K1030ac/K1033ac)
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-6g0p:
Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated E2F1 peptide (K117ac/K120ac)
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-6g0q:
Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated GATA1 peptide (K312ac/K315ac)
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-6g0r:
Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated POLR2A peptide (K775ac/K778ac)
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-6g0s:
Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated SIRT7 peptide (K272ac/K275ac)
Method: X-RAY DIFFRACTION / Resolution: 1.48 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / Bromodomain / complex / Structural Genomics / Structural Genomics Consortium / SGC

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