期刊
FEBS LETTERS
卷 592, 期 7, 页码 1185-1201出版社
WILEY
DOI: 10.1002/1873-3468.13015
关键词
HOXA1; HOX proteins; OGT; Post-translational modifications; protein-protein interaction
资金
- Concerted Research Action 'Action de Recherche Concertee' (ARC) [12/17 - 041]
- Fonds Speciaux de Recherche' of the Universite catholique de Louvain
- FRS-FNRS
HOXA1 belongs to the HOX family of transcription factors which are key regulators of animal development. Little is known about the molecular pathways controlling HOXA1. Recent data from our group revealed distinct partner proteins interacting with HOXA1. Among them, OGT is an O-linked N-acetylglucosamine (O-GlcNAc) transferase modifying a variety of proteins involved in different cellular processes including transcription. Here, we confirm OGT as a HOXA1 interactor, we characterise which domains of HOXA1 and OGT are required for the interaction, and we provide evidence that OGT post-translationally modifies HOXA1. Mass spectrometry experiments indeed reveal that HOXA1 can be phosphorylated on the AGGTVGSPQYIHHSY peptide and that upon OGT expression, the phosphate adduct is replaced by an O-GlcNAc group.
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