[HTML][HTML] Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
EG Mimnaugh, C Chavany, L Neckers - Journal of Biological Chemistry, 1996 - ASBMB
Treatment of SKBr3 human breast carcinoma cells with the benzoquinoid ansamycin,
geldanamycin, rapidly depletes p185 c-erbB-2 protein-tyrosine kinase. Loss of p185 c-erbB-
2 is initiated by disruption of a heteromeric complex between p185 c-erbB-2 and the 94-kDa
glucose-regulated protein, GRP94, to which geldanamycin binds avidly. Here we report that
within minutes of exposure to geldanamycin, mature p185 c-erbB-2 becomes
polyubiquitinated. Treatment of cells with the specific proteasome proteolytic inhibitor …
geldanamycin, rapidly depletes p185 c-erbB-2 protein-tyrosine kinase. Loss of p185 c-erbB-
2 is initiated by disruption of a heteromeric complex between p185 c-erbB-2 and the 94-kDa
glucose-regulated protein, GRP94, to which geldanamycin binds avidly. Here we report that
within minutes of exposure to geldanamycin, mature p185 c-erbB-2 becomes
polyubiquitinated. Treatment of cells with the specific proteasome proteolytic inhibitor …