Characterization of the Relationship between the Chaperone and Lipid-Binding Functions of the 70-kDa Heat-Shock Protein, HspA1A

Characterization of the Relationship between the Chaperone and Lipid-Binding Functions of the 70-kDa Heat-Shock Protein, HspA1A

HspA1A, a molecular chaperone, translocates to the plasma membrane (PM) of stressed and cancer cells. This translocation results in HspA1A’s cell-surface presentation, which renders tumors radiation insensitive. To specifically inhibit the lipid-driven HspA1A’s PM translocation and devise new therap...

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Bibliographic Details
Main Authors: Larissa Smulders, Amanda J. Daniels, Caroline B. Plescia, Devon Berger, Robert V. Stahelin, Nikolas Nikolaidis
Format: Article
Language:English
Published: MDPI AG 2020-08-01
Series:International Journal of Molecular Sciences
Subjects:
chaperone function
heat-shock proteins
lipid binding
phosphatidylserine
protein refolding
Online Access:https://www.mdpi.com/1422-0067/21/17/5995

Internet

https://www.mdpi.com/1422-0067/21/17/5995

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