BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.
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ABSTRACT:
SUBMITTER: Gray F
PROVIDER: S-EPMC5105191 | biostudies-literature | 2016 Nov
REPOSITORIES: biostudies-literature
Publications
BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.
Gray Felicia F Cho Hyo Je HJ Shukla Shirish S He Shihan S Harris Ashley A Boytsov Bohdan B Jaremko Łukasz Ł Jaremko Mariusz M Demeler Borries B Lawlor Elizabeth R ER Grembecka Jolanta J Cierpicki Tomasz T
Nature communications 20161109
BMI1 is a core component of the polycomb repressive complex 1 (PRC1) and emerging data support a role of BMI1 in cancer. The central domain of BMI1 is involved in protein-protein interactions and is essential for its oncogenic activity. Here, we present the structure of BMI1 bound to the polyhomeotic protein PHC2 illustrating that the central domain of BMI1 adopts an ubiquitin-like (UBL) fold and binds PHC2 in a β-hairpin conformation. Unexpectedly, we find that the UBL domain is involved in hom ...[more]
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