Major histocompatibility (MHC) class II molecules are transmembrane proteins that have a central role in development and control of the immune system. The protein encoded by this gene, along with regulatory factor X-associated protein and regulatory factor-5, forms a complex that binds to the X box motif of certain MHC class II gene promoters and activates their transcription. Once bound to the promoter, this complex associates with the non-DNA-binding factor MHC class II transactivator, which controls the cell type specificity and inducibility of MHC class II gene expression. This protein contains ankyrin repeats involved in protein-protein interactions. Mutations in this gene have been linked to bare lymphocyte syndrome type II, complementation group B. Two transcript variants encoding different isoforms have been described for this gene, with only one isoform showing activation activity.[3]
↑Masternak K, Barras E, Zufferey M, Conrad B, Corthals G, Aebersold R, Sanchez JC, Hochstrasser DF, Mach B, Reith W (Nov 1998). "A gene encoding a novel RFX-associated transactivator is mutated in the majority of MHC class II deficiency patients". Nature Genetics. 20 (3): 273–7. doi:10.1038/3081. PMID9806546.
↑Nagarajan UM, Louis-Plence P, DeSandro A, Nilsen R, Bushey A, Boss JM (Feb 1999). "RFX-B is the gene responsible for the most common cause of the bare lymphocyte syndrome, an MHC class II immunodeficiency". Immunity. 10 (2): 153–62. doi:10.1016/S1074-7613(00)80016-3. PMID10072068.
Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID8889548.
Lin JH, Makris A, McMahon C, Bear SE, Patriotis C, Prasad VR, Brent R, Golemis EA, Tsichlis PN (May 1999). "The ankyrin repeat-containing adaptor protein Tvl-1 is a novel substrate and regulator of Raf-1". The Journal of Biological Chemistry. 274 (21): 14706–15. doi:10.1074/jbc.274.21.14706. PMID10329666.
Nagarajan UM, Peijnenburg A, Gobin SJ, Boss JM, van den elsen PJ (Apr 2000). "Novel mutations within the RFX-B gene and partial rescue of MHC and related genes through exogenous class II transactivator in RFX-B-deficient cells". Journal of Immunology. 164 (7): 3666–74. doi:10.4049/jimmunol.164.7.3666. PMID10725724.
Wiszniewski W, Fondaneche MC, Lambert N, Masternak K, Picard C, Notarangelo L, Schwartz K, Bal J, Reith W, Alcaide C, de Saint Basile G, Fischer A, Lisowska-Grospierre B (Apr 2000). "Founder effect for a 26-bp deletion in the RFXANK gene in North African major histocompatibility complex class II-deficient patients belonging to complementation group B". Immunogenetics. 51 (4–5): 261–7. doi:10.1007/s002510050619. PMID10803838.
Dimberg J, Hugander A, Häll-Karlsson BM, Sirsjö A (Mar 2002). "RFX-B, a MHC class II transcription factor, suppressed in human colorectal adenocarcinomas". International Journal of Molecular Medicine. 9 (3): 213–6. doi:10.3892/ijmm.9.3.213. PMID11836625.
Wiszniewski W, Fondaneche MC, Louise-Plence P, Prochnicka-Chalufour A, Selz F, Picard C, Le Deist F, Eliaou JF, Fischer A, Lisowska-Grospierre B (Feb 2003). "Novel mutations in the RFXANK gene: RFX complex containing in-vitro-generated RFXANK mutant binds the promoter without transactivating MHC II". Immunogenetics. 54 (11): 747–55. doi:10.1007/s00251-002-0521-1. PMID12618906.
Wang AH, Grégoire S, Zika E, Xiao L, Li CS, Li H, Wright KL, Ting JP, Yang XJ (Aug 2005). "Identification of the ankyrin repeat proteins ANKRA and RFXANK as novel partners of class IIa histone deacetylases". The Journal of Biological Chemistry. 280 (32): 29117–27. doi:10.1074/jbc.M500295200. PMID15964851.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC1847948. PMID17353931.
