| Literature DB >> 23036489 |
Tarryn Willmer1, Lara Contu, Gregory L Blatch, Adrienne L Edkins.
Abstract
The Hsp90/Hsp70 organising protein (Hop) is a co-chaperone that mediates the interaction of Hsp90 and Hsp70 molecular chaperones during assembly of Hsp90 complexes in cells. Formation of Hsp90 complexes is a key intermediate step in the maturation and homeostasis of oncoproteins and several hormone receptors. In this paper, we demonstrate that knockdown of Hop decreased migration of Hs578T and MDA-MB-231 breast cancer cells. Hop was identified in isolated pseudopodia fractions; it colocalised with actin in lamellipodia, and co-sedimented with purified actin in vitro. Knockdown of Hop caused a decrease in the level of RhoC GTPase, and significantly inhibited pseudopodia formation in Hs578T cells. Our data suggest that Hop regulates directional cell migration by multiple unknown mechanisms.Entities:
Mesh：
Substances：
Year: 2012 PMID： 23036489 DOI： 10.1016/j.canlet.2012.09.021
Source DB: PubMed Journal: Cancer Lett ISSN： 0304-3835 Impact factor: 8.679