Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2047429 | FEBS Letters | 2015 | 7 Pages |
Abstract
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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Authors
Benedikt Nimmervoll, Lilia A. Chtcheglova, Kata Juhasz, Nunilo Cremades, Francesco A. Aprile, Alois Sonnleitner, Peter Hinterdorfer, Laszlo Vigh, Johannes Preiner, Zsolt Balogi,