Biology:DNAJB6
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
DnaJ homolog subfamily B member 6 is a protein that in humans is encoded by the DNAJB6 gene.[1][2][3]
Function
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.[3]
Interactions
DNAJB6 has been shown to interact with keratin 18.[4] 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.[5] 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.[6]
References
- ↑ "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. June 1999. doi:10.1007/s100380050139. PMID 10319584.
- ↑ "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. January 1999. doi:10.1074/jbc.274.5.3151. PMID 9915854.
- ↑ 3.0 3.1 "Entrez Gene: DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10049.
- ↑ "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. November 2000. doi:10.1074/jbc.M003492200. PMID 10954706.
- ↑ "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. November 2014. doi:10.1074/jbc.M114.595124. PMID 25217638.
- ↑ "Inhibition of DNAJ-HSP70 interaction improves strength in muscular dystrophy". The Journal of Clinical Investigation 130 (8): 4470–4485. August 2020. doi:10.1172/JCI136167. PMID 32427588.
Further reading
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "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. November 2000. doi:10.1074/jbc.M003492200. PMID 10954706.
- "DNA cloning using in vitro site-specific recombination". Genome Research 10 (11): 1788–95. November 2000. doi:10.1101/gr.143000. PMID 11076863.
- "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature". Cell Stress & Chaperones 5 (2): 98–112. April 2000. doi:10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2. PMID 11147971.
- "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. March 2001. doi:10.1101/gr.GR1547R. PMID 11230166.
- "Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently". The Journal of Biological Chemistry 277 (22): 19831–8. May 2002. doi:10.1074/jbc.M109613200. PMID 11896048.
- "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. September 2002. doi:10.1042/BJ20011717. PMID 12069690.
- "Characterization of two isoforms of a human DnaJ homologue, HSJ2". Molecular Biology Reports 30 (3): 149–53. September 2003. doi:10.1023/A:1024916223616. PMID 12974469.
- "[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. November 2003. PMID 15182641.
- "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. January 2005. doi:10.1095/biolreprod.104.030866. PMID 15342353.
- "From ORFeome to biology: a functional genomics pipeline". Genome Research 14 (10B): 2136–44. October 2004. doi:10.1101/gr.2576704. PMID 15489336.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. October 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "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. November 2005. doi:10.1128/MCB.25.22.9936-9948.2005. PMID 16260608.
- "The unhappy chaperone". QRB Discovery (Cambridge University Press) 2: e7. 2021. doi:10.1017/qrd.2021.5. PMID 37529680.
External links
- DNAJB6 human gene location in the UCSC Genome Browser.
- DNAJB6 human gene details in the UCSC Genome Browser.
 |  |
