Elevated levels of ribosomal proteins eL36 and eL42 control expression of Hsp90 in rhabdomyosarcoma

Mammalian 90 kDa heat shock protein (Hsp90) is a ubiquitous molecular chaperone whose expression is selectively upregulated during stress, although the precise control mechanism of this increase is yet to be fully elucidated. We used polysome profiling to show that Hsp90α mRNA is selectively transla...

Full description

Saved in:
Bibliographic Details
Published inTranslation (Austin, Tex.) Vol. 4; no. 2; p. e1244395
Main Authors Shaikho, Sarah, Dobson, Christine C., Naing, Thet, Samanfar, Bahram, Moteshareie, Houman, Hajikarimloo, Maryam, Golshani, Ashkan, Holcik, Martin
Format Journal Article
LanguageEnglish
Published United States Taylor & Francis 01.01.2016
Subjects
cancer
drug resistance
heat shock
Research Paper
ribosomal protein
selective translation
heat shock
cancer
ribosomal protein
drug resistance
selective translation
Online AccessGet full text

Cover

More Information
Summary:Mammalian 90 kDa heat shock protein (Hsp90) is a ubiquitous molecular chaperone whose expression is selectively upregulated during stress, although the precise control mechanism of this increase is yet to be fully elucidated. We used polysome profiling to show that Hsp90α mRNA is selectively translated, while global translation is inhibited during heat stress. Furthermore, we have identified 2 ribosomal proteins, eL36 and eL42 that modulate Hsp90α expression under both normal and heat shock conditions. Importantly, we noted that expression of eL36 and eL42 is elevated in a panel of human rhabdomyosarcomas where it drives high expression of Hsp90 and modulates sensitivity of these cells to an Hsp90 inhibitor 17-AAG.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Note. The ribosomal protein nomenclature used throughout the manuscript is as proposed in Ban et al.,1
ISSN:2169-074X
2169-0731
2169-0731
DOI:10.1080/21690731.2016.1244395