Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins

@inproceedings{Smith2015RestrictingDI,
  title={Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins},
  author={Jennifer R. Smith and Emmanuel de Billy and Stephen M. Hobbs and Marissa V Powers and Chrisostomos Prodromou and Laurence H. Pearl and Paul A Clarke and Paul Workman},
  booktitle={Oncogene},
  year={2015}
}
The HSP90 molecular chaperone plays a key role in the maturation, stability and activation of its clients, including many oncogenic proteins. Kinases are a substantial and important subset of clients requiring the key cochaperone CDC37. We sought an improved understanding of protein kinase chaperoning by CDC37 in cancer cells. CDC37 overexpression in human colon cancer cells increased CDK4 protein levels, which was negated upon CDC37 knockdown. Overexpressing CDC37 increased CDK4 protein half… CONTINUE READING
Highly Cited
This paper has 18 citations. REVIEW CITATIONS
Related Discussions
This paper has been referenced on Twitter 30 times. VIEW TWEETS

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

The Mysterious Ways of ErbB2/HER2 Trafficking

Membranes • 2014
View 11 Excerpts
Highly Influenced

References

Publications referenced by this paper.
Showing 1-10 of 48 references

Similar Papers

Loading similar papers…