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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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DNAJB2  -  DnaJ (Hsp40) homolog, subfamily B, member 2

Homo sapiens

Synonyms: DSMA5, DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, HSJ-1, HSJ1, ...
 
 
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High impact information on DNAJB2

  • Furthermore, we demonstrated that the J-domain of two human DnaJ homologs, HSJ1 or DNAJ2, could substitute functionally for the amino-terminus of TAg in promoting viral DNA replication [1].
  • HSJ1 combines a J-domain that stimulates substrate loading onto the Hsc70 chaperone with ubiquitin interaction motifs (UIMs) involved in binding ubiquitylated chaperone clients [2].
  • Because of their enrichment at the site of rhodopsin production, we investigated the effect of HSJ1 isoforms on the cellular processing of wild-type and mutant rhodopsin apoprotein in SK-N-SH cells [3].
  • These results strongly suggest that HSJ1 proteins interfere with an endogenous DnaJ-like protein that is involved in uncoating [4].
  • Assignment of the neuronal cochaperone, HSJ1, to human chromosome bands 2q32-->q34 between D2S295 and D2S339 by in situ hybridization and somatic cell and radiation hybrids [5].
 

Biological context of DNAJB2

  • In order to measure the kinetics of clathrin release from coated vesicles, we have developed a quantitative, two-site ELISA for clathrin triskelions and demonstrated that stoichiometric amounts of HSJ1 proteins inhibit the initial burst of hsc70-mediated clathrin uncoating by over 40% [4].

References

  1. DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication. Campbell, K.S., Mullane, K.P., Aksoy, I.A., Stubdal, H., Zalvide, J., Pipas, J.M., Silver, P.A., Roberts, T.M., Schaffhausen, B.S., DeCaprio, J.A. Genes Dev. (1997) [Pubmed]
  2. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Westhoff, B., Chapple, J.P., van der Spuy, J., Höhfeld, J., Cheetham, M.E. Curr. Biol. (2005) [Pubmed]
  3. The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. Chapple, J.P., Cheetham, M.E. J. Biol. Chem. (2003) [Pubmed]
  4. Inhibition of hsc70-catalysed clathrin uncoating by HSJ1 proteins. Cheetham, M.E., Anderton, B.H., Jackson, A.P. Biochem. J. (1996) [Pubmed]
  5. Assignment of the neuronal cochaperone, HSJ1, to human chromosome bands 2q32-->q34 between D2S295 and D2S339 by in situ hybridization and somatic cell and radiation hybrids. Chapple, J.P., Hardcastle, A.J., Kurzik-Dumke, U., Collier, D.A., Cheetham, M.E. Cytogenet. Cell Genet. (1999) [Pubmed]
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