MLX (gene)
From Wikipedia the free encyclopedia
Max-like protein X is a protein that in humans is encoded by the MLX gene.[5][6]
Function
[edit]The product of this gene belongs to the family of basic helix-loop-helix leucine zipper (bHLH-Zip) transcription factors. These factors form heterodimers with Mad proteins and play a role in proliferation, determination and differentiation. This gene product may act to diversify Mad family function by its restricted association with a subset of the Mad family of transcriptional repressors, namely Mad1 and Mad4. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.[6]
Interactions
[edit]MLX (gene) has been shown to interact with MNT,[7][8] MXD1[7][8] and MLXIPL.[7]
MLX must dimerize with MondoA[9] or with MLXIPL (carbohydrate-responsive element-binding protein) to regulate target genes.[10]
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000108788 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017801 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Bjerknes M, Cheng H (November 1996). "TCFL4: a gene at 17q21.1 encoding a putative basic helix-loop-helix leucine-zipper transcription factor". Gene. 181 (1–2): 7–11. doi:10.1016/S0378-1119(96)00376-9. PMID 8973301.
- ^ a b "Entrez Gene: MLX MAX-like protein X".
- ^ a b c Cairo S, Merla G, Urbinati F, Ballabio A, Reymond A (March 2001). "WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network". Human Molecular Genetics. 10 (6): 617–27. doi:10.1093/hmg/10.6.617. PMID 11230181.
- ^ a b Meroni G, Cairo S, Merla G, Messali S, Brent R, Ballabio A, Reymond A (July 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene. 19 (29): 3266–77. doi:10.1038/sj.onc.1203634. PMID 10918583. S2CID 17891130.
- ^ Kaadige MR, Yang J, Wilde BR, Ayer DE (2015). "MondoA-Mlx transcriptional activity is limited by mTOR-MondoA interaction". Molecular and Cellular Biology. 35 (1): 101–110. doi:10.1128/MCB.00636-14. PMC 4295369. PMID 25332233.
- ^ Song Z, Yang H, Zhou L, Yang F (2019). "Glucose-Sensing Transcription Factor MondoA/ChREBP as Targets for Type 2 Diabetes: Opportunities and Challenges". International Journal of Molecular Sciences. 20 (20): E5132. doi:10.3390/ijms20205132. PMC 6829382. PMID 31623194.
Further reading
[edit]- Rommens JM, Durocher F, McArthur J, Tonin P, LeBlanc JF, Allen T, Samson C, Ferri L, Narod S, Morgan K (August 1995). "Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21". Genomics. 28 (3): 530–42. doi:10.1006/geno.1995.1185. PMID 7490091.
- Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M (September 1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Research. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
- Billin AN, Eilers AL, Queva C, Ayer DE (December 1999). "Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors". The Journal of Biological Chemistry. 274 (51): 36344–50. doi:10.1074/jbc.274.51.36344. PMID 10593926.
- Meroni G, Cairo S, Merla G, Messali S, Brent R, Ballabio A, Reymond A (July 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene. 19 (29): 3266–77. doi:10.1038/sj.onc.1203634. PMID 10918583. S2CID 17891130.
- Billin AN, Eilers AL, Coulter KL, Logan JS, Ayer DE (December 2000). "MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network". Molecular and Cellular Biology. 20 (23): 8845–54. doi:10.1128/MCB.20.23.8845-8854.2000. PMC 86535. PMID 11073985.
- Cairo S, Merla G, Urbinati F, Ballabio A, Reymond A (March 2001). "WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network". Human Molecular Genetics. 10 (6): 617–27. doi:10.1093/hmg/10.6.617. PMID 11230181.
- Eilers AL, Sundwall E, Lin M, Sullivan AA, Ayer DE (December 2002). "A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex". Molecular and Cellular Biology. 22 (24): 8514–26. doi:10.1128/MCB.22.24.8514-8526.2002. PMC 139889. PMID 12446771.
- Merla G, Howald C, Antonarakis SE, Reymond A (July 2004). "The subcellular localization of the ChoRE-binding protein, encoded by the Williams-Beuren syndrome critical region gene 14, is regulated by 14-3-3". Human Molecular Genetics. 13 (14): 1505–14. doi:10.1093/hmg/ddh163. PMID 15163635.
- Ma L, Tsatsos NG, Towle HC (March 2005). "Direct role of ChREBP.Mlx in regulating hepatic glucose-responsive genes". The Journal of Biological Chemistry. 280 (12): 12019–27. doi:10.1074/jbc.M413063200. PMID 15664996.
- Sans CL, Satterwhite DJ, Stoltzman CA, Breen KT, Ayer DE (July 2006). "MondoA-Mlx heterodimers are candidate sensors of cellular energy status: mitochondrial localization and direct regulation of glycolysis". Molecular and Cellular Biology. 26 (13): 4863–71. doi:10.1128/MCB.00657-05. PMC 1489152. PMID 16782875.
External links
[edit]- MLX+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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