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

Zsolt Balogi, Gabrielle Multhoff, Thomas Kirkegaard Jensen, Emyr Lloyd-Evans, Tetsumori Yamashima, Marja Jäättelä, John L. Harwood, L. Vígh

Research output: Contribution to journalReview article

10 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)18-30
Number of pages13
JournalProgress in Lipid Research
Volume74
DOIs
Publication statusPublished - Apr 1 2019

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

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  • Cite this

    Balogi, Z., Multhoff, G., Jensen, T. K., Lloyd-Evans, E., Yamashima, T., Jäättelä, M., Harwood, J. L., & Vígh, L. (2019). Hsp70 interactions with membrane lipids regulate cellular functions in health and disease. Progress in Lipid Research, 74, 18-30. https://doi.org/10.1016/j.plipres.2019.01.004