@Article{096504018X15154104709325,
AUTHOR = {Bui Thi Kim Ly, Hoang Thanh Chi},
TITLE = {ETV6/FLT3 Fusion Is a Novel Client Protein of Hsp90},
JOURNAL = {Oncology Research},
VOLUME = {26},
YEAR = {2018},
NUMBER = {8},
PAGES = {1201--1205},
URL = {http://www.techscience.com/or/v26n8/56735},
ISSN = {1555-3906},
ABSTRACT = {FMS-like tyrosine kinase-3 fragments from exon 14 to the end without any mutations or deletions have been 
reported to fuse to ETV6 (TEL) in a few cases of myeloid/lymphoid neoplasms with eosinophilia carrying a 
translocation t(12;13)(p13;q12). This fusion protein confers constitutive activation on the FLT3 fragment and 
induces factor-independent growth in transfected Ba/F3 cells, indicating that it is an oncoprotein. However, the 
mechanism controlling the stability of this oncoprotein is unknown. In this study, we focus on finding factors 
controlling the stability of ETV6/FLT3. We have shown that the stability of ETV6/FLT3 is regulated by the 
Hsp90 chaperone. ETV6/FLT3 fusion protein forms a complex with Hsp90 by coimmunoprecipitation analyses using an Hsp90 antibody. The association between ETV6/FLT3 fusion protein and Hsp90 was impaired 
after treating ETV6/FLT3 transient transfection cos7 cells with 17-allylamino-17-demethoxygeldanamycin 
(17-AAG). 17-AAG induced a time- and dose-dependent downregulation of ectopically expressed ETV6/FLT3 
protein in cos7 and HeLa-transfected cells. By using cycloheximide to block new protein translation, we found 
that 17-AAG accelerated the decay of ETV6/FLT3. Our findings could contribute to more understanding of the 
ETV6/FLT3 regulation through Hsp90 chaperone and open the way to finding effective treatment strategies 
for this rare disease.},
DOI = {10.3727/096504018X15154104709325}
}