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 |
Journal | FEBS letters
(FEBS Lett)
Vol. 589
Issue 19 Pt B
Pg. 2747-53
(Sep 14 2015)
ISSN: 1873-3468 [Electronic] England |
PMID | 26257049
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
Chemical References |
- Clathrin
- HSP70 Heat-Shock Proteins
- Protein Aggregates
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Topics |
- Animals
- Cell Line, Tumor
- Clathrin
(metabolism)
- Endocytosis
- HSP70 Heat-Shock Proteins
(chemistry, metabolism)
- Melanoma, Experimental
(metabolism, pathology)
- Membrane Microdomains
- Mice
- Protein Aggregates
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