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Cell surface localised Hsp70 is a cancer specific regulator of clathrin‐independent endocytosis
Author(s) -
Nimmervoll Benedikt,
Chtcheglova Lilia A.,
Juhasz Kata,
Cremades Nunilo,
Aprile Francesco A.,
Sonnleitner Alois,
Hinterdorfer Peter,
Vigh Laszlo,
Preiner Johannes,
Balogi Zsolt
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.07.037
Subject(s) - endocytosis , lipid raft , clathrin , microbiology and biotechnology , cell , cancer cell , cell membrane , chemistry , hsp70 , biology , cancer , heat shock protein , biochemistry , signal transduction , genetics , gene
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.