IRF2BP2 binds to a conserved RxSVI motif of protein partners and regulates megakaryocytic differentiation.

ABSTRACT: IRF2BP2 is a transcriptional coregulator that plays diverse regulatory roles in various cellular processes in either IRF2-dependent or IRF2-independent manner through interactions with protein partners via its RING domain; however, the underlying molecular mechanisms remain unclear. In this study, we conduct a motif discovery search on the sequences of interacting proteins IRF2 and VGLL4 of IRF2BP2 and identify a conserved RxSVI motif. Biochemical and structural data reveal that the RING domain binds to the motif-containing peptides of IRF2 and VGLL4 with comparable affinities and in a similar manner. The motif-containing peptides tend to form a short loop along with a short β-strand, which facilitates effective recognition and tight binding by the RING domain. Further exploration of this

SUBMITTER: Wang G 

PROVIDER: S-EPMC11608337 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature