Title : RET is a heat shock protein 90 (HSP90) client protein and is knocked down upon HSP90 pharmacological block.

Pub. Date : 2010 Jul

PMID : 20444924






8 Functional Relationships(s)
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1 OBJECTIVE: Our aim was to investigate whether RET protein half-life depends on HSP90 and to dissect the molecular pathway responsible for the degradation of RET upon HSP90 inhibition by 17-AAG. tanespimycin ret proto-oncogene Homo sapiens
2 OBJECTIVE: Our aim was to investigate whether RET protein half-life depends on HSP90 and to dissect the molecular pathway responsible for the degradation of RET upon HSP90 inhibition by 17-AAG. tanespimycin ret proto-oncogene Homo sapiens
3 RESULTS: 17-AAG induced a 26S proteasome-dependent degradation of wild-type RET and MEN2-associated RET mutants. tanespimycin ret proto-oncogene Homo sapiens
4 RESULTS: 17-AAG induced a 26S proteasome-dependent degradation of wild-type RET and MEN2-associated RET mutants. tanespimycin ret proto-oncogene Homo sapiens
5 17-AAG blocked RET downstream effectors and RET-dependent transcriptional activation of gene promoters. tanespimycin ret proto-oncogene Homo sapiens
6 17-AAG blocked RET downstream effectors and RET-dependent transcriptional activation of gene promoters. tanespimycin ret proto-oncogene Homo sapiens
7 CONCLUSION: RET and MEN2-associated RET mutants rely on HSP90 for protein stability, and HSP90 blockade by 17-AAG promotes RET degradation. tanespimycin ret proto-oncogene Homo sapiens
8 CONCLUSION: RET and MEN2-associated RET mutants rely on HSP90 for protein stability, and HSP90 blockade by 17-AAG promotes RET degradation. tanespimycin ret proto-oncogene Homo sapiens