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ALYREF

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Aly/REF export factor, also known as THO complex subunit 4 is a protein that in humans is encoded by the ALYREF gene.{{cite journal | vauthors = Muravenko OV, Gizatullin RZ, Al-Amin AN, Protopopov AI, Kashuba VI, Zelenin AV, Zabarovsky ER | title = Human ALY/BEF gene Map position 17q25.3 | journal = Chromosome Res | volume = 8 | issue = 6 | pages = 562 |date=Jan 2001 | pmid = 11032328 | doi =10.1023/A:1009236126053 | s2cid = 6859937 }}{{cite web | title = Entrez Gene: ALYREF Aly/REF export factor| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10189}}

The ALYREF gene encodes Aly/REF export factor (ALY; THO complex subunit 4, Tho4; RNA and export factor binding protein 1, Refbp1), a ubiquitously expressed nuclear protein that functions as a molecular chaperone and export adapter involved in nuclear export of spliced and unspliced mRNA. The TRanscription-EXport (TREX) complex, a key player in mRNA export, includes the THO subcomplex, the RNA helicase UAP56, and the RNA-binding protein ALY. In yeast, TREX is recruited co-transcriptionally; in human cells it is recruited during a late step of splicing. The human TREX complex is recruited to a region near the 5' end of mRNA by interaction of ALY and THO with the nuclear cap-binding complex. As a chaperone, ALY promotes dimerization of transcription factors containing basic leucine zipper (bZIP) domains.,{{cite web | title = Entrez Gene: THOC4 THO complex 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10189}} thereby promoting transcriptional activation. ALY has key roles in 3'-end processing of polyadenylated mRNAs and in nuclear export of both polyadenylated and non-polyadenylated mRNAs.{{cite journal | vauthors = Shi M, Zhang H, Wu X, He Z, Wang L, Yin S, Tian B, Li G, Cheng H | title = ALYREF mainly binds to the 5' and the 3' regions of the mRNA in vivo. | journal = Nucleic Acids Res | volume = 45 | issue = 16 | pages = 9640–9653 |date=Sep 2017 | pmid = 28934468 | pmc = 5766156 | doi =10.1093/nar/gkx597 }}{{cite journal | vauthors = Shi M, Zhang H, Wu X, He Z, Wang L, Yin S, Tian B, Li G, Cheng H | title = ALYREF links 3'-end processing to nuclear export of non-polyadenylated mRNAs. | journal = EMBO J | volume = 38 | issue = 9 | pages = e99910 |date=Mar 2019 | pmid = 30858280 | pmc = 6484419| doi =10.15252/embj.201899910 }} After mRNA binds to ALY, it is apparently transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). The full-length ALY protein (Refbp1-I, 255 amino acids encoded by six exons{{cite web | title = Ensembl: Gene ALYREF ENSG00000183684 (human)| url = http://uswest.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000183684;r=17:81887844-81891586}}) has a conserved RNA recognition motif (RRM; amino acids 105-182) flanked by alanine/arginine/glycine-rich sequences; an N-terminal region (amino acids 16-37) is sufficient for RNA binding and interaction with the NXF1-NXT1 heterodimer.{{cite web | title = UniProtKB Q86V81 (THOC4_HUMAN)| url = https://www.uniprot.org/uniprot/Q86V81}}

References

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Further reading

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  • {{cite journal | vauthors=Bruhn L, Munnerlyn A, Grosschedl R |title=ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function. |journal=Genes Dev. |volume=11 |issue= 5 |pages= 640–53 |year= 1997 |pmid= 9119228 |doi=10.1101/gad.11.5.640 |doi-access=free }}
  • {{cite journal | vauthors=Neubauer G, King A, Rappsilber J |title=Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 46–50 |year= 1998 |pmid= 9731529 |doi= 10.1038/1700 |s2cid=585778 |display-authors=etal}}
  • {{cite journal | vauthors=Wichmann I, Garcia-Lozano JR, Respaldiza N |title=Autoantibodies to transcriptional regulation proteins DEK and ALY in a patient with systemic lupus erythematosus. |journal=Hum. Immunol. |volume=60 |issue= 1 |pages= 57–62 |year= 1999 |pmid= 9952027 |doi=10.1016/S0198-8859(98)00085-8 |display-authors=etal}}
  • {{cite journal | vauthors=Virbasius CM, Wagner S, Green MR |title=A human nuclear-localized chaperone that regulates dimerization, DNA binding, and transcriptional activity of bZIP proteins. |journal=Mol. Cell |volume=4 |issue= 2 |pages= 219–28 |year= 1999 |pmid= 10488337 |doi=10.1016/S1097-2765(00)80369-X |doi-access=free }}
  • {{cite journal | vauthors=Le Hir H, Izaurralde E, Maquat LE, Moore MJ |title=The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. |journal=EMBO J. |volume=19 |issue= 24 |pages= 6860–9 |year= 2001 |pmid= 11118221 |doi= 10.1093/emboj/19.24.6860 | pmc=305905 }}
  • {{cite journal | vauthors=Kim VN, Kataoka N, Dreyfuss G |title=Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex. |journal=Science |volume=293 |issue= 5536 |pages= 1832–6 |year= 2001 |pmid= 11546873 |doi= 10.1126/science.1062829 |bibcode=2001Sci...293.1832K |s2cid=12018200 }}
  • {{cite journal | vauthors=Luo ML, Zhou Z, Magni K |title=Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly. |journal=Nature |volume=413 |issue= 6856 |pages= 644–7 |year= 2001 |pmid= 11675789 |doi= 10.1038/35098106 |bibcode=2001Natur.413..644L |s2cid=4395388 |display-authors=etal}}
  • {{cite journal | vauthors=Kataoka N, Diem MD, Kim VN |title=Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex. |journal=EMBO J. |volume=20 |issue= 22 |pages= 6424–33 |year= 2002 |pmid= 11707413 |doi= 10.1093/emboj/20.22.6424 | pmc=125744 |display-authors=etal}}
  • {{cite journal | vauthors=Strässer K, Masuda S, Mason P |title=TREX is a conserved complex coupling transcription with messenger RNA export. |journal=Nature |volume=417 |issue= 6886 |pages= 304–8 |year= 2002 |pmid= 11979277 |doi= 10.1038/nature746 |bibcode=2002Natur.417..304S |s2cid=1112194 |display-authors=etal}}
  • {{cite journal | vauthors=Jurica MS, Licklider LJ, Gygi SR |title=Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. |journal=RNA |volume=8 |issue= 4 |pages= 426–39 |year= 2002 |pmid= 11991638 |doi=10.1017/S1355838202021088 | pmc=1370266 |display-authors=etal}}
  • {{cite journal | vauthors=Rappsilber J, Ryder U, Lamond AI, Mann M |title=Large-scale proteomic analysis of the human spliceosome. |journal=Genome Res. |volume=12 |issue= 8 |pages= 1231–45 |year= 2002 |pmid= 12176931 |doi= 10.1101/gr.473902 | pmc=186633 }}
  • {{cite journal | vauthors=Chen IH, Sciabica KS, Sandri-Goldin RM |title=ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway. |journal=J. Virol. |volume=76 |issue= 24 |pages= 12877–89 |year= 2002 |pmid= 12438613 |doi=10.1128/JVI.76.24.12877-12889.2002 | pmc=136725 }}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=McCracken S, Longman D, Johnstone IL |title=An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation. |journal=J. Biol. Chem. |volume=278 |issue= 45 |pages= 44153–60 |year= 2004 |pmid= 12944400 |doi= 10.1074/jbc.M306856200 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Pryor A, Tung L, Yang Z |title=Growth-regulated expression and G0-specific turnover of the mRNA that encodes URH49, a mammalian DExH/D box protein that is highly related to the mRNA export protein UAP56. |journal=Nucleic Acids Res. |volume=32 |issue= 6 |pages= 1857–65 |year= 2004 |pmid= 15047853 |doi= 10.1093/nar/gkh347 | pmc=390356 |display-authors=etal}}
  • {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
  • {{cite journal | vauthors=Ong SE, Mittler G, Mann M |title=Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. |journal=Nat. Methods |volume=1 |issue= 2 |pages= 119–26 |year= 2005 |pmid= 15782174 |doi= 10.1038/nmeth715 |s2cid=6654604 }}
  • {{cite journal | vauthors=Masuda S, Das R, Cheng H |title=Recruitment of the human TREX complex to mRNA during splicing. |journal=Genes Dev. |volume=19 |issue= 13 |pages= 1512–7 |year= 2005 |pmid= 15998806 |doi= 10.1101/gad.1302205 | pmc=1172058 |display-authors=etal}}
  • {{cite journal | vauthors=Mertz JA, Kobayashi R, Dudley JP |title=ALY is a common coactivator of RUNX1 and c-Myb on the type B leukemogenic virus enhancer. |journal=J. Virol. |volume=81 |issue= 7 |pages= 3503–13 |year= 2007 |pmid= 17229714 |doi= 10.1128/JVI.02253-06 | pmc=1866045 }}
  • {{cite journal | vauthors=Quaresma AJ, Sievert R, Nickerson JA |title=Regulation of mRNA export by the PI3 kinase/AKT signal transduction pathway. |journal=Mol. Biol. Cell |volume= 24|issue= 8 |pages= 1208–21 |year= 2013 |pmid= 23427269 |doi= 10.1091/mbc.E12-06-0450 | pmc=3623641 }}

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External links

  • {{UCSC genome browser|ALYREF}}
  • {{UCSC gene details|ALYREF}}
  • {{PDBe-KB2|Q86V81|THO complex subunit 4}}

{{PDB Gallery|geneid=10189}}

{{gene-17-stub}}