Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein
Authors:Abbey D. Zuehlke1 and Leonard Neckers1
doi: 10.15698/mic2017.08.586
Volume 4, pp. 273 to 274, published 01/08/2017.
1 Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Keywords:
Co-chaperone, posttranslational modification, ATPase cycle, client protein.
Corresponding Author(s):
Conflict of interest statement:
The authors declare no conflict of interest.
Please cite this article as:
Abbey D. Zuehlke and Leonard Neckers (2017). Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein. Microbial Cell 4(8): 273-274. doi: 10.15698/mic2017.08.586
© 2017 Zuehlke and Neckers. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
Abstract:
Redundant functions maintained from single to multicellular organisms have made Saccharomyces cerevisiae an important model for the analysis of conserved complex cellular processes. Yeast have been especially useful in understanding the regulation and function of the essential molecular chaperone, Heat Shock Protein 90 (Hsp90). Research focused on Hsp90 has determined that it is highly regulated by both co-chaperones and posttranslational modifications. A recent study performed by (Zuehlke et al., 2017) demonstrates that the function of one co-chaperone in yeast is replaced by posttranslational modification (PTM) of a single amino acid within Hsp90 in higher eukaryotes.