Target intelligence / Profile preview

Double PHD fingers 1 (DPF1)

Target
DPF1
Molecular classification
Chromatin remodeling protein, Transcription factor/interacting protein, Zinc finger protein, Epigenetic regulator (component of SWI/SNF complex, specifically neuron-specific nBAF complex)
01

Overview

Double PHD fingers 1 (DPF1) is a neuron-enriched chromatin remodeling factor that mediates gene expression by recognizing specific histone modifications through its tandem PHD domains. It is part of the neuron-specific nBAF (SWI/SNF) complex, regulating neuronal differentiation and survival as neural progenitors exit mitosis. DPF1's activity is crucial for enabling transcriptional programs required for nervous system development, where its PHD fingers selectively bind acetylated and crotonylated histone H3 tails, thereby modulating chromatin structure and gene accessibility. Defects or dysregulation in DPF1 or related SWI/SNF components can result in neurodevelopmental syndromes and may have roles, as inferred from the PHD finger protein family, in cancer biology via epigenetic mechanisms[2][3][4][1].

Other names
BAF45BNEUD4Zinc finger protein neuro-d4SMARCG1BRG1-associated factor 45BD4neuro-d4 homolog
02

Mechanism of action

Not applicable (no proven DPF1-targeting mechanism for existing drugs; in theory, inhibition or modulation would affect chromatin state and neuronal gene transcription)

03

Biological functions

Chromatin remodelingRegulation of gene expressionNervous system development (especially neuronal differentiation)Regulation of cell survival
04

Disease associations

Neurodevelopmental disorders (Nicolaides-Baraitser Syndrome, cerebellar hypoplasia, multinucleated neurons)Cancer (by analogy to PHD finger proteins in general, which may act as oncogenic drivers or tumor suppressors; direct links for DPF1 may still be under investigation)
05

Safety considerations

Potential off-target effects in therapies modulating chromatin remodelersRisk of impaired neurodevelopment or cell survival if DPF1 function is inhibited

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