Skip to main content

Charting the landscape of tandem BRCT domain-mediated protein interactions.

Publication ,  Journal Article
Woods, NT; Mesquita, RD; Sweet, M; Carvalho, MA; Li, X; Liu, Y; Nguyen, H; Thomas, CE; Iversen, ES; Marsillac, S; Karchin, R; Koomen, J; Monteiro, ANA
Published in: Science signaling
September 2012

Eukaryotic cells have evolved an intricate system to resolve DNA damage to prevent its transmission to daughter cells. This system, collectively known as the DNA damage response (DDR) network, includes many proteins that detect DNA damage, promote repair, and coordinate progression through the cell cycle. Because defects in this network can lead to cancer, this network constitutes a barrier against tumorigenesis. The modular BRCA1 carboxyl-terminal (BRCT) domain is frequently present in proteins involved in the DDR, can exist either as an individual domain or as tandem domains (tBRCT), and can bind phosphorylated peptides. We performed a systematic analysis of protein-protein interactions involving tBRCT in the DDR by combining literature curation, yeast two-hybrid screens, and tandem affinity purification coupled to mass spectrometry. We identified 23 proteins containing conserved BRCT domains and generated a human protein-protein interaction network for seven proteins with tBRCT. This study also revealed previously unknown components in DNA damage signaling, such as COMMD1 and the target of rapamycin complex mTORC2. Additionally, integration of tBRCT domain interactions with DDR phosphoprotein studies and analysis of kinase-substrate interactions revealed signaling subnetworks that may aid in understanding the involvement of tBRCT in disease and DNA repair.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Science signaling

DOI

EISSN

1937-9145

ISSN

1945-0877

Publication Date

September 2012

Volume

5

Issue

242

Start / End Page

rs6

Related Subject Headings

  • TOR Serine-Threonine Kinases
  • Sequence Analysis, Protein
  • Protein Structure, Tertiary
  • Phosphorylation
  • Peptides
  • Multiprotein Complexes
  • Mechanistic Target of Rapamycin Complex 2
  • Humans
  • DNA Repair
  • DNA Damage
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Woods, N. T., Mesquita, R. D., Sweet, M., Carvalho, M. A., Li, X., Liu, Y., … Monteiro, A. N. A. (2012). Charting the landscape of tandem BRCT domain-mediated protein interactions. Science Signaling, 5(242), rs6. https://doi.org/10.1126/scisignal.2002255
Woods, Nicholas T., Rafael D. Mesquita, Michael Sweet, Marcelo A. Carvalho, Xueli Li, Yun Liu, Huey Nguyen, et al. “Charting the landscape of tandem BRCT domain-mediated protein interactions.Science Signaling 5, no. 242 (September 2012): rs6. https://doi.org/10.1126/scisignal.2002255.
Woods NT, Mesquita RD, Sweet M, Carvalho MA, Li X, Liu Y, et al. Charting the landscape of tandem BRCT domain-mediated protein interactions. Science signaling. 2012 Sep;5(242):rs6.
Woods, Nicholas T., et al. “Charting the landscape of tandem BRCT domain-mediated protein interactions.Science Signaling, vol. 5, no. 242, Sept. 2012, p. rs6. Epmc, doi:10.1126/scisignal.2002255.
Woods NT, Mesquita RD, Sweet M, Carvalho MA, Li X, Liu Y, Nguyen H, Thomas CE, Iversen ES, Marsillac S, Karchin R, Koomen J, Monteiro ANA. Charting the landscape of tandem BRCT domain-mediated protein interactions. Science signaling. 2012 Sep;5(242):rs6.

Published In

Science signaling

DOI

EISSN

1937-9145

ISSN

1945-0877

Publication Date

September 2012

Volume

5

Issue

242

Start / End Page

rs6

Related Subject Headings

  • TOR Serine-Threonine Kinases
  • Sequence Analysis, Protein
  • Protein Structure, Tertiary
  • Phosphorylation
  • Peptides
  • Multiprotein Complexes
  • Mechanistic Target of Rapamycin Complex 2
  • Humans
  • DNA Repair
  • DNA Damage