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Publication : The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome.

First Author  Kleijnen MF Year  2000
Journal  Mol Cell Volume  6
Issue  2 Pages  409-19
PubMed ID  10983987 Mgi Jnum  J:64191
Mgi Id  MGI:1888843 Doi  10.1016/s1097-2765(00)00040-x
Citation  Kleijnen MF, et al. (2000) The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. Mol Cell 6(2):409-19
abstractText  Although there is a binding site on the proteasome for the polyubiquitin chains attached to degradation substrates by the ubiquitination machinery, it is currently unclear whether in vivo the activities of the ubiquitination machinery and the proteasome are coupled. Here we show that two human homologs of the yeast ubiquitin-like Dsk2 protein, hPLIC-1 and hPLIC-2, physically associate with both proteasomes and ubiquitin ligases in large complexes. Overexpression of hPLIC proteins interferes with the in vivo degradation of two unrelated ubiquitin-dependent proteasome substrates, p53 and IkappaBalpha, but not a ubiquitin-independent substrate. Our findings raise the possibility that the hPLIC proteins, and possibly related ubiquitin-like family members, may functionally link the ubiquitination machinery to the proteasome to affect in vivo protein degradation.
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