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The O‐GlcNAc transferase OGT interacts with and post‐translationally modifies the transcription factor HOXA 1
Author(s) -
Draime Amandine,
Bridoux Laure,
Belpaire Magali,
Pringels Tamara,
Degand Hervé,
Morsomme Pierre,
Rezsohazy René
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13015
Subject(s) - transcription factor , transferase , transcription (linguistics) , chemistry , microbiology and biotechnology , biology , biochemistry , gene , enzyme , linguistics , philosophy
HOXA 1 belongs to the HOX family of transcription factors which are key regulators of animal development. Little is known about the molecular pathways controlling HOXA 1. Recent data from our group revealed distinct partner proteins interacting with HOXA 1. 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 HOXA 1 interactor, we characterise which domains of HOXA 1 and OGT are required for the interaction, and we provide evidence that OGT post‐translationally modifies HOXA 1. Mass spectrometry experiments indeed reveal that HOXA 1 can be phosphorylated on the AGGTVGSPQYIHHSY peptide and that upon OGT expression, the phosphate adduct is replaced by an O‐GlcNAc group.