Fig. 2.

Oxidation of nonhistone proteins by lysyl oxidases. LOX oxidases can deaminate several intracellular substrates, allowing them to regulate protein function, localization, stability, and/or interactions. (i) TAF10, a member of the TFIID complex, can be oxidized by LOXL2, which alters its interaction with other members of the TFIID complex and leads to its release from pluripotency gene promoters in embryonic stem cells. (ii) LOXL3 deacetylates and deacetyliminates the transcription factor STAT3 on multiple acetyl‐lysine sites, disrupting its dimerization and inhibiting its transcriptional activity. (iii) Several studies suggest that the transcription factor SNAIL1 can be oxidized by LOXL2/3; this posttranslational modification could lead to an undefined conformational change that would protect SNAIL1 from nuclear export and/or proteasomal degradation. In addition, LOXL2 could also oxidize acetylated SNAIL1, thereby regulating its interactions with corepressors and expression of its target genes. (v) LOXL2/3 can be auto‐oxidized as a way to regulate its own enzymatic activity in response to treatment with trihydrophenolics. (v) The bFGF is oxidized by LOX, resulting in spontaneous and covalent crosslinking of bFGF monomers and the inhibition of its nuclear localization and mitogenic potential through ERK1/2MAP kinase activation. (vi) The transcriptional coactivator VGLL3 is oxidized by cytoplasmic LOX in myogenic progenitors; this modification promotes the translocation of VGLL3 into the nucleus, where it binds MEF2 and TEF and modulates large gene expression programs.