Analyses have associated variations in MDGA genes with schizophrenia, bipolar disorder and autism spectrum disorder. Taken together, our study demonstrates the key transcriptional role of Laf4 during cortical cell migration that is relevant to the haploinsufficiency and silencing associated with human neurodevelopmental disorders. The redox-regulated transcription factor SoxR is present in a diverse range of Proteobacteria and Actinobacteria and homologs are highly similar at the amino acid level. SoxR homologs function as homodimers and have a conserved amino-terminal helix-turn-helix DNA binding domain, suggesting that these proteins bind to and regulate transcription from similar operator sequences. This has been confirmed in organisms where SoxR has been biochemically characterized. SoxR homologs also share a conserved sequence in the carboxy-terminus that has been shown to be necessary for coordinating centers in SoxR proteins from Escherichia coli, Pseudomonas aeruginosa, and Streptomyces coelicolor. These clusters are central to SoxR’s ability to detect changes in the cellular redox environment and regulate gene expression in response. SoxR was originally discovered in the enterobacterium E. coli where it promotes resistance to redoxcycling drugs like paraquat and menadione. Subsequent studies Temozolomide 85622-93-1 revealed that in this microorganism SoxR mediates its effects in a two-step process. Upon sensing redox stress via its clusters, SoxR activates the expression of a second transcription factor, soxS. SoxS, an AraC-type regulator then recruits RNA polymerase to the promoters of.100 genes, whose protein products cumulatively restore redox homeostasis and repair oxidant-induced cellular damage. The E. coli SoxRS regulon is conserved in other enterobacteria where it functions to confer generalized protection against exogenous redox-cycling compounds. Various lines of research conducted in the past decade indicate that this function may be limited to members of the Enterobacteriaceae, and that the SoxR regulatory network is different in other bacteria. A comprehensive bioinformatic survey of sequenced bacterial genomes revealed that while a soxR homolog is detected in 176 genomes, a soxS homolog is present only in enteric bacteria where it appears to be the solitary gene directly regulated by SoxR. The same study showed that in non-enterics, SoxR is predicted to directly regulate a small number of genes. In further contrast to the apparent function of SoxR in enteric bacteria, none of the putative SoxR targets in non-enterics encode proteins that are typically involved in oxidative stress detoxification and repair. Instead these genes encode membrane transporters and enzymes with homology to proteins that modify small molecules, including antibiotics. The absence of a soxS homolog and the predicted SoxR regulons in non-enterics has given rise to the notion that SoxR does not regulate a generalized oxidative stress response in the majority of bacteria. This has been corroborated for Pseudomonas putida, P. aeruginosa, and S. coelicolor, where deletion of soxR does not result in increased sensitivity to redoxcycling drugs when compared to the parental strain.