Disease relevance of MLXIPL

• WBSCR14, a putative transcription factor gene deleted in Williams-Beuren syndrome: complete characterisation of the human gene and the mouse ortholog [1].

Psychiatry related information on MLXIPL

• Adaptive behavior following subliminal stimulation with "Mommy and I are One" (MIO) is a poorly understood finding [2].

High impact information on MLXIPL

• We identified five novel WBSCR14-interacting proteins, four 14-3-3 isotypes and NIF3L1, which form a single polypeptide complex in mammalian cells [3].
• The WBSCR14 gene, one of the genes mapping to the WBS critical region, encodes a member of the basic-helix-loop-helix leucine zipper family of transcription factors, which dimerizes with the Max-like protein, Mlx [3].
• WBSCR14 forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence CACGTG [4].
• Modern analytical methods, theoretical calculations and molecular biology tools have given further insight into the mode of action of MIO [5].
• Here, we describe mutational experiments in GFP designed to convert this chromophore into a 4-methylidene-imidazole-5-one (MIO) moiety similar to the post-translational active-site electrophile of histidine ammonia lyase (HAL) [6].

Biological context of MLXIPL

• The WBSCR14 locus encompasses 33 kb of genomic DNA with 17 exons [1].
• WS-betaTRP has four putative beta-transducin (WD40) repeats, and WS-bHLH is a novel basic helix-loop-helix leucine zipper (bHLHZip) gene [7].
• The presence of MIO in the active site is supported by several lines of evidence [8].
• At present little is known about the transcriptional targets of MondoA; however, pyruvate kinase is a putative target of MondoB/CHREBP/WBSCR14, suggesting a function for the Mondo family in glucose and/or lipid metabolism [9].
• Corethane 80A displayed the best overall resistance to hydrolysis, ESC, MIO and calcification, followed by ChronoFlex 80A and PHMO-PU [10].

Associations of MLXIPL with chemical compounds

• Previously, we established that SgcC4 is an aminomutase that catalyzes the conversion of L-tyrosine to (S)-beta-tyrosine and employs 4-methylideneimidazole-5-one (MIO) at its active site [Christenson, S. D., Liu, W., Toney, M. D., and Shen, B. (2003) J. Am. Chem. Soc. 125, 6062-6063] [8].
• Histidine ammonia-lyase (EC 4.3.1.3) catalyzes the nonoxidative elimination of the alpha-amino group of histidine using a 4-methylidene-imidazole-5-one (MIO), which is formed autocatalytically from the internal peptide segment 142Ala-Ser-Gly [11].
• Here, we show that, in contrast to the former assumption, ammonia in the complex is not covalently bound to the prosthetic electrophile, 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO; 5) [12].
• In vitro tests in H(2)O(2) solution indicated that both SME's accelerated MIO [13].
• A new polycarbonate polyurethane has superior biostability in early in vivo qualification tests compared to the polyether polyurethanes, including no evidence of hydrolysis, ESC or MIO [14].

Analytical, diagnostic and therapeutic context of MLXIPL

• These procedures in psychoanalytic treatment seem similar to a subliminal MIO message and to the subliminal exposure of a happy face, as mentioned above in the fMRI study by Whalen et al [15].
• Both ammonia-lyases have a catalytically important electrophilic group, which was believed to be dehydroalanine for 30 years but has now been revealed by X-ray crystallography and UV spectroscopy to be a highly electrophilic 5-methylene-3,5-dihydroimidazol-4-one (MIO) group [16].

References