WDR5
WDR5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | WDR5, BIG-3, CFAP89, SWD3, WD repeat-containing protein 5, WD repeat domain 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 609012; MGI: 2155884; HomoloGene: 59931; GeneCards: WDR5; OMA:WDR5 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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WD repeat-containing protein 5 is a protein that in humans is encoded by the WDR5 gene.[5][6]
This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 7 WD repeats. Alternatively spliced transcript variants encoding the same protein have been identified.[6]
Interactions
WDR5 has been shown to interact with Host cell factor C1[7][8] and MLL.[7] It also interacts with the long non-coding RNA HOTTIP and to the lncRNA NeST.[9][10] WDR5 is a key determinant for MYC recruitment to chromatin[11]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000196363 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026917 – 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.
- ^ Gori F, Divieti P, Demay MB (Dec 2001). "Cloning and characterization of a novel WD-40 repeat protein that dramatically accelerates osteoblastic differentiation". J Biol Chem. 276 (49): 46515–22. doi:10.1074/jbc.M105757200. PMID 11551928.
- ^ a b "Entrez Gene: WDR5 WD repeat domain 5".
- ^ a b Yokoyama, Akihiko; Wang Zhong; Wysocka Joanna; Sanyal Mrinmoy; Aufiero Deborah J; Kitabayashi Issay; Herr Winship; Cleary Michael L (Jul 2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Mol. Cell. Biol. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. ISSN 0270-7306. PMC 480881. PMID 15199122.
- ^ Wysocka, Joanna; Myers Michael P; Laherty Carol D; Eisenman Robert N; Herr Winship (Apr 2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. ISSN 0890-9369. PMC 196026. PMID 12670868.
- ^ Wells, Alexandria C.; Pobezinskaya, Elena L.; Pobezinsky, Leonid A. (April 2020). "Non-coding RNAs in CD8 T cell biology". Molecular Immunology. 120: 67–73. doi:10.1016/j.molimm.2020.01.023. ISSN 1872-9142. PMC 7093237. PMID 32085976.
- ^ Wang KC, Yang YW, Liu B, Sanyal A, Corces-Zimmerman R, Chen Y, et al. (2011). "A long noncoding RNA maintains active chromatin to coordinate homeotic gene expression". Nature. 472 (7341): 120–4. Bibcode:2011Natur.472..120W. doi:10.1038/nature09819. PMC 3670758. PMID 21423168.
- ^ Thomas, L. R.; Tansey, W. P. (2015). "Interaction with WDR5 Promotes Target Gene Recognition and Tumorigenesis by MYC". Molecular Cell. 58 (3): 1–13. doi:10.1016/j.molcel.2015.02.028. PMC 4427524. PMID 25818646.
Further reading
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Wysocka J, Myers MP, Laherty CD, et al. (2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
- Gori F, Demay MB (2004). "BIG-3, a novel WD-40 repeat protein, is expressed in the developing growth plate and accelerates chondrocyte differentiation in vitro". Endocrinology. 145 (3): 1050–4. doi:10.1210/en.2003-1314. PMID 14657013.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Yokoyama A, Wang Z, Wysocka J, et al. (2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Mol. Cell. Biol. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. PMC 480881. PMID 15199122.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
- Wysocka J, Swigut T, Milne TA, et al. (2005). "WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development". Cell. 121 (6): 859–72. doi:10.1016/j.cell.2005.03.036. PMID 15960974. S2CID 17521631.
- Dou Y, Milne TA, Tackett AJ, et al. (2005). "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF". Cell. 121 (6): 873–85. doi:10.1016/j.cell.2005.04.031. PMID 15960975. S2CID 14717470.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
- Gori F, Friedman L, Demay MB (2006). "Wdr5, a novel WD repeat protein, regulates osteoblast and chondrocyte differentiation in vivo". Journal of Musculoskeletal & Neuronal Interactions. 5 (4): 338–9. PMID 16340128.
- Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
- Ruthenburg AJ, Wang W, Graybosch DM, et al. (2006). "Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex". Nat. Struct. Mol. Biol. 13 (8): 704–12. doi:10.1038/nsmb1119. PMC 4698793. PMID 16829959.
- Couture JF, Collazo E, Trievel RC (2006). "Molecular recognition of histone H3 by the WD40 protein WDR5". Nat. Struct. Mol. Biol. 13 (8): 698–703. doi:10.1038/nsmb1116. PMID 16829960. S2CID 26165068.
- Dou Y, Milne TA, Ruthenburg AJ, et al. (2006). "Regulation of MLL1 H3K4 methyltransferase activity by its core components". Nat. Struct. Mol. Biol. 13 (8): 713–9. doi:10.1038/nsmb1128. PMID 16878130. S2CID 12849159.
- Schuetz A, Allali-Hassani A, Martín F, et al. (2006). "Structural basis for molecular recognition and presentation of histone H3 by WDR5". EMBO J. 25 (18): 4245–52. doi:10.1038/sj.emboj.7601316. PMC 1570438. PMID 16946699.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
- Bryan AF, Wang J, Howard GC, et al. (2020). "WDR5 is a conserved regulator of protein synthesis gene expression". Nucleic Acids Research. 48 (6): 2924–2941. doi:10.1093/nar/gkaa051. PMC 7102967. PMID 31996893.
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- 2cnx: WDR5 AND HISTONE H3 LYSINE 4 DIMETHYL COMPLEX AT 2.1 ANGSTROM
- 2co0: WDR5 AND UNMODIFIED HISTONE H3 COMPLEX AT 2.25 ANGSTROM
- 2g99: Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5
- 2g9a: Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5
- 2gnq: Structure of wdr5
- 2h13: Crystal structure of WDR5/histone H3 complex
- 2h14: Crystal of WDR5 (apo-form)
- 2h68: Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
- 2h6k: Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
- 2h6n: Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
- 2h6q: Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
- 2h9l: WDR5delta23
- 2h9m: WDR5 in complex with unmodified H3K4 peptide
- 2h9n: WDR5 in complex with monomethylated H3K4 peptide
- 2h9p: WDR5 in complex with trimethylated H3K4 peptide
- 2o9k: WDR5 in Complex with Dimethylated H3K4 Peptide
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