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

Benedikt Nimmervoll, Lilia A. Chtcheglova, Kata Juhasz, Nunilo Cremades, Francesco A. Aprile, Alois Sonnleitner, Peter Hinterdorfer, Laszlo Vigh, Johannes Preiner, Zsolt Balogi

Research output: Contribution to journalArticle

21 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 - Sep 14 2015

Keywords

  • Cancer
  • Clustering
  • Endocytosis
  • Hsp70
  • Membrane

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Nimmervoll, B., Chtcheglova, L. A., Juhasz, K., Cremades, N., Aprile, F. A., Sonnleitner, A., Hinterdorfer, P., Vigh, L., Preiner, J., & Balogi, Z. (2015). Cell surface localised Hsp70 is a cancer specific regulator of clathrin-independent endocytosis. FEBS letters, 589(19), 2747-2753. https://doi.org/10.1016/j.febslet.2015.07.037