Nature Communications (Nov 2016)

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization

  • Felicia Gray,
  • Hyo Je Cho,
  • Shirish Shukla,
  • Shihan He,
  • Ashley Harris,
  • Bohdan Boytsov,
  • Łukasz Jaremko,
  • Mariusz Jaremko,
  • Borries Demeler,
  • Elizabeth R. Lawlor,
  • Jolanta Grembecka,
  • Tomasz Cierpicki

DOI
https://doi.org/10.1038/ncomms13343
Journal volume & issue
Vol. 7, no. 1
pp. 1 – 12

Abstract

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BMI1, a core element of the polycomb repressive complex 1, is suggested to have oncogenic activity in a variety of cancers. Here, the authors report the structure of BMI1 bound to the protein PHC2, identify BMI1 homo-oligomerization interfaces, and analyse the role of BMI1 protein-protein interactions in PRC1 function.