Hsp70 interactions with membrane lipids regulate cellular functions in health and disease

• Published in: Progress in lipid research Vol. 74; pp. 18 - 30
• Main Authors: Balogi, Zsolt, Multhoff, Gabriele, Jensen, Thomas Kirkegaard, Lloyd-Evans, Emyr, Yamashima, Tetsumori, Jäättelä, Marja, Harwood, John L., Vígh, László
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.04.2019
• ISSN: 0163-7827; 1873-2194
• DOI: 10.1016/j.plipres.2019.01.004

Beyond guarding the cellular proteome the major stress inducible heat shock protein Hsp70 has been shown to interact with lipids. Non-cytosolic Hsp70 stabilizes membranes during stress challenges and, in pathophysiological states, facilitates endocytosis, counteracts apoptotic mechanisms, sustains survival pathways or represents a signal that can be recognized by the immune system. Disease-coupled lipid-associated functions of Hsp70 may be targeted via distinct subcellular localizations of Hsp70 itself or its specific interacting lipids. With a special focus on interacting lipids, here we discuss localization-dependent roles of the membrane-bound Hsp70 in the context of its therapeutic potential, particularly in cancer and neurodegenerative diseases.