Cell surface localised Hsp70 is a cancer specific regulator of clathrin-independent endocytosis
2015
Nimmervoll, Benedikt | Chtcheglova, Lilia A. | Juhasz, Kata | Cremades, Nunilo | Aprile, Francesco A. | Sonnleitner, Alois | Hinterdorfer, Peter | Vígh, László | Preiner, Johannes | Balogi, Zsolt
The stress inducible heat shock protein 70 (Hsp70) is present specifically on the tumour cell surface yet without a pro-tumour function revealed. We show here that cell surface localised Hsp70 (sHsp70) supports clathrin-independent endocytosis (CIE) in melanoma models. Remarkably, ability of Hsp70 to cluster on lipid rafts in vitro correlated with larger nano-domain sizes of sHsp70 in high sHsp70 expressing cell membranes. Interfering with Hsp70 oligomerisation impaired sHsp70-mediated facilitation of endocytosis. Altogether our findings suggest that a sub-fraction of sHsp70 co-localising with lipid rafts enhances CIE through oligomerisation and clustering. Targeting or utilising this tumour specific mechanism may represent an additional benefit for anti-cancer therapy.
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