Cell surface localised Hsp70 is a cancer specific regulator of clathrin-independent endocytosis

Benedikt Nimmervoll, Lilia Chtcheglova, Kata Juhasz, N Cremades, F.A. Aprile, Alois Sonnleitner, Peter Hinterdorfer, L. Vigh, Johannes Preiner, Zolt Balogi

Research output: Contribution to journalArticle

24 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)2747-2753
Number of pages7
JournalFEBS Letters
Volume589
Issue number19
DOIs
Publication statusPublished - 14 Sep 2015

Keywords

  • Cancer
  • Clustering
  • Endocytosis
  • Hsp70
  • Membrane

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