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GFP-PHF23 interactome in HeLa nuclear lysate

ABSTRACT: PHF23 is a methyl reading protein with its PHD domain. We found PHF23 represses autophagy performed purification and identification of PHF23 interactome.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Seon Ah Choi

LAB HEAD: Sung Hee Baek

PROVIDER: PXD065543 | Pride | 2025-12-15

REPOSITORIES: Pride

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			Action	DRS
	GFP-23_bead_01.raw	Raw
	GFP-23_bead_mzML.mzML	Mzml
	GFP_bead_01.raw	Raw
	GFP_bead_mzML.mzML	Mzml
	checksum.txt	Txt

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Publications

Dual mechanism of autophagy gene repression by PHF23 and therapeutic potential of its inhibition in protein aggregation disorders.

Choi Seon Ah SA Kim Jaebeom J Yu Young Suk YS Kim Jaemin J Kim Se In SI Bae Hamin H Kwon Junhee J Kim Keun Il KI Baek Sung Hee SH

Nucleic acids research 20251101 22

Autophagy is a conserved self-digestion pathway essential for maintaining cellular homeostasis. While the transcriptional and epigenetic activation of autophagy under nutrient-deprived condition is well studied, the repression mechanisms of autophagy under basal conditions remain poorly understood. Here, we identify plant homeodomain finger protein 23 (PHF23) as an epigenetic repressor of autophagy through a CRISPR interference screen. Importantly, PHF23 inhibits autophagy gene expression via tw ...[more]

PMID: 41359382

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Integrated phosphoproteome, ubiquitinome, and acetylome analyses uncovering the post-translational modifications crosstalk during MSP1-induced signaling in rice

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USF2 interacted proteins in HEK293T cells

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Spliceosome disassembly factors ILP1 and NTR1 promote microRNA biogenesis in Arabidopsis

Project description:A battery of spliceosome-associated proteins has been identified in microRNA (miRNA) biogenesis; however, the underlying mechanisms remain elusive. The intron lariat spliceosome (ILS) complex is highly conserved among eukaryotes and its disassembly marks the end of a canonical splicing cycle. In this study, we show that two conserved disassembly factors of the ILS complex, ILP1 and NTR1, positively regulate microRNA biogenesis through facilitating transcriptional elongation in Arabidopsis. ILP1 and NTR1 form a stable complex and co-regulate alternative splicing of more than a hundred genes across the genome including the core circadian gene LHY and some pri-miRNAs. Dysfunction in either ILP1 or NTR1 result in reduced RNA polymerase II occupancy at elongated regions of MIR chromatins, without affecting MIR promoter activity, pri-miRNA decay and DCL1 processing. Our results provide insights into the molecular mechanisms of spliceosomal machineries in non-coding RNA regulation.

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BS3 intermolecular crosslinking map of SAGA and SLIK (SAGA-like) transcription coactivators

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Lysiphlebus fabarum (Hymenoptera: Braconidae: Aphidiinae) venom proteomic analysis

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Proteome of Agave angustifolia Haw.: insights about metabolism of amino acids in albino plantlets

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