Structural highlights
Function
[REQU_HUMAN] May be a transcription factor required for the apoptosis response following survival factor withdrawal from myeloid cells. Might also have a role in the development and maturation of lymphoid cells.
Publication Abstract from PubMed
Double plant homeodomain finger 2 (DPF2) is a highly evolutionarily conserved member of the d4 protein family that is ubiquitously expressed in human tissues and was recently shown to inhibit the myeloid differentiation of hematopoietic stem/progenitor and acute myelogenous leukemia cells. Here, we present the crystal structure of the tandem plant homeodomain finger domain of human DPF2 at 1.6-A resolution. We show that DPF2 interacts with the acetylated tails of both histones 3 and 4 via bipartite binding pockets on the DPF2 surface. Blocking these interactions through targeted mutagenesis of DPF2 abolishes its recruitment to target chromatin regions as well as its ability to prevent myeloid differentiation in vivo. Our findings suggest that the histone binding of DPF2 plays an important regulatory role in the transcriptional program that drives myeloid differentiation.
Histone-binding of DPF2 mediates its repressive role in myeloid differentiation.,Huber FM, Greenblatt SM, Davenport AM, Martinez C, Xu Y, Vu LP, Nimer SD, Hoelz A Proc Natl Acad Sci U S A. 2017 Jun 6;114(23):6016-6021. doi:, 10.1073/pnas.1700328114. Epub 2017 May 22. PMID:28533407[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huber FM, Greenblatt SM, Davenport AM, Martinez C, Xu Y, Vu LP, Nimer SD, Hoelz A. Histone-binding of DPF2 mediates its repressive role in myeloid differentiation. Proc Natl Acad Sci U S A. 2017 Jun 6;114(23):6016-6021. doi:, 10.1073/pnas.1700328114. Epub 2017 May 22. PMID:28533407 doi:http://dx.doi.org/10.1073/pnas.1700328114
