Balogi, Zsolt, Multhoff, Gabrielle, Jensen, Thomas Kirkegaard, Lloyd-Evans, Emyr ![]() ![]() |
Preview |
PDF
- Accepted Post-Print Version
Available under License Creative Commons Attribution Non-commercial No Derivatives. Download (1MB) | Preview |
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
Item Type: | Article |
---|---|
Date Type: | Publication |
Status: | Published |
Schools: | Biosciences |
Publisher: | Elsevier |
ISSN: | 0163-7827 |
Date of First Compliant Deposit: | 14 February 2019 |
Date of Acceptance: | 28 January 2019 |
Last Modified: | 19 Nov 2024 05:45 |
URI: | https://orca.cardiff.ac.uk/id/eprint/119542 |
Citation Data
Cited 58 times in Scopus. View in Scopus. Powered By Scopus® Data
Actions (repository staff only)
![]() |
Edit Item |