Hsp70 in cancer: role of the membrane-anchored chaperone.

Fiche publication


Date publication

octobre 2019

Journal

Cancer letters

Auteurs

Membres identifiés du Cancéropôle Est :
Dr GARRIDO Carmen, Dr GOBBO Jessica


Tous les auteurs :
Elmallah MIY, Cordonnier M, Vautrot V, Chanteloup G, Garrido C, Gobbo J

Résumé

Hsp70 is a highly conserved and inducible heat shock protein that belongs to the HSP70 family of molecular chaperones and plays a central role in protein homeostasis. The main function of Hsp70 is to protect cells from physiological, pathological and environmental insults, as it assists an ATP-dependent manner the process of protein folding. Since Hsp70 provides critical cell survival functions, cancer cells are assumed to rely on this chaperone. Strong evidence suggests that Hsp70 is upregulated in different type of cancers and is involved in tumor growth, invasion, migration and resistance to anti-cancer therapy. Interestingly, this Hsp70 upregulation induces Hsp70 re-location into plasma membrane. In this review, the role of Hsp70 in cancer will be discussed focusing particularly on the extracellular membrane-bound Hsp70. The mechanism by which Hsp70 is translocated to plasma membrane of tumor cells and the recent discoveries of drugs targeting this Hsp70 in cancer therapy will be also highlighted.

Mots clés

Cancer, Hsp70 translocation, Targeting Hsp70, membrane Hsp70

Référence

Cancer Lett.. 2019 Oct 25;: