DNAJB6
DnaJ homolog subfamily B member 6 is a protein that in humans is encoded by the DNAJB6 gene.
Function
[edit]This gene encodes a member of the DNAJ protein family. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. This family member may also play a role in polyglutamine aggregation in specific neurons. Alternative splicing of this gene results in multiple transcript variants; however, not all variants have been fully described.[7]
Interactions
[edit]DNAJB6 has been shown to interact with keratin 18.[8] It has been also shown that the aggregation of Aβ42 (a process involved in e.g. Alzheimer's disease) is retarded by DNAJB6 in a concentration-dependent manner, extending to very low sub-stoichiometric molar ratios of chaperone to peptide.[9] Dominant mutations in DNAJB6 have also been found to cause a late-onset muscle disease termed limb-girdle muscular dystrophy type D1 (LGMDD1), which is characterized by protein aggregation and vacuolar myopathology.[10]
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000105993 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029131 – 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.
- ^ Seki N, Hattori A, Hayashi A, Kozuma S, Miyajima N, Saito T (June 1999). "Cloning, tissue expression, and chromosomal assignment of human MRJ gene for a member of the DNAJ protein family". Journal of Human Genetics. 44 (3): 185–9. doi:10.1007/s100380050139. PMID 10319584.
- ^ Pei L (January 1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells". The Journal of Biological Chemistry. 274 (5): 3151–8. doi:10.1074/jbc.274.5.3151. PMID 9915854.
- ^ a b "Entrez Gene: DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6".
- ^ Izawa I, Nishizawa M, Ohtakara K, Ohtsuka K, Inada H, Inagaki M (November 2000). "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein". The Journal of Biological Chemistry. 275 (44): 34521–7. doi:10.1074/jbc.M003492200. PMID 10954706.
- ^ Månsson C, Arosio P, Hussein R, Kampinga HH, Hashem RM, Boelens WC, Dobson CM, Knowles TP, Linse S, Emanuelsson C (November 2014). "Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation". The Journal of Biological Chemistry. 289 (45): 31066–76. doi:10.1074/jbc.M114.595124. PMC 4223311. PMID 25217638.
- ^ Bengoechea R, Findlay AR, Bhadra AK, Shao H, Stein KC, Pittman SK, Daw JA, Gestwicki JE, True HL, Weihl CC (August 2020). "Inhibition of DNAJ-HSP70 interaction improves strength in muscular dystrophy". The Journal of Clinical Investigation. 130 (8): 4470–4485. doi:10.1172/JCI136167. PMC 7410071. PMID 32427588.
Further reading
[edit]- Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Izawa I, Nishizawa M, Ohtakara K, Ohtsuka K, Inada H, Inagaki M (November 2000). "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein". The Journal of Biological Chemistry. 275 (44): 34521–7. doi:10.1074/jbc.M003492200. PMID 10954706.
- Hartley JL, Temple GF, Brasch MA (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Ohtsuka K, Hata M (April 2000). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature". Cell Stress & Chaperones. 5 (2): 98–112. doi:10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2 (inactive 1 November 2024). PMC 312896. PMID 11147971.
{{cite journal}}: CS1 maint: DOI inactive as of November 2024 (link) - Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
- Chuang JZ, Zhou H, Zhu M, Li SH, Li XJ, Sung CH (May 2002). "Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently". The Journal of Biological Chemistry. 277 (22): 19831–8. doi:10.1074/jbc.M109613200. PMID 11896048.
- Farinha CM, Nogueira P, Mendes F, Penque D, Amaral MD (September 2002). "The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70". The Biochemical Journal. 366 (Pt 3): 797–806. doi:10.1042/BJ20011717. PMC 1222832. PMID 12069690.
- Hanai R, Mashima K (September 2003). "Characterization of two isoforms of a human DnaJ homologue, HSJ2". Molecular Biology Reports. 30 (3): 149–53. doi:10.1023/A:1024916223616. PMID 12974469. S2CID 24105834.
- Liu Y, Zhu MC, Wang YJ, Zhan Z, Liu CG (November 2003). "[Cloning of a DnaJ homolog chaperon PBP and its subcellular localization]". Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi = Chinese Journal of Cellular and Molecular Immunology. 19 (6): 531–4. PMID 15182641.
- Berruti G, Martegani E (January 2005). "The deubiquitinating enzyme mUBPy interacts with the sperm-specific molecular chaperone MSJ-1: the relation with the proteasome, acrosome, and centrosome in mouse male germ cells". Biology of Reproduction. 72 (1): 14–21. doi:10.1095/biolreprod.104.030866. PMID 15342353.
- Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (October 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
- Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 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.
- Dai YS, Xu J, Molkentin JD (November 2005). "The DnaJ-related factor Mrj interacts with nuclear factor of activated T cells c3 and mediates transcriptional repression through class II histone deacetylase recruitment". Molecular and Cellular Biology. 25 (22): 9936–48. doi:10.1128/MCB.25.22.9936-9948.2005. PMC 1280278. PMID 16260608.
- Linse S, Thalberg K, Knowles TP (2021). "The unhappy chaperone". QRB Discovery. 2. Cambridge University Press: e7. doi:10.1017/qrd.2021.5. PMC 10392682. PMID 37529680.
External links
[edit]- DNAJB6 human gene location in the UCSC Genome Browser.
- DNAJB6 human gene details in the UCSC Genome Browser.