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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bieganowski, Pawel Synoradzki, Kamil |
| Description | Author Affiliation: Synoradzki K ( Department of Experimental Pharmacology, Mossakowski Medical Research Centre, Polish Academy of Sciences, 5 Pawinskiego St., Warsaw 02-106, Poland.); Bieganowski P ( Department of Experimental Pharmacology, Mossakowski Medical Research Centre, Polish Academy of Sciences, 5 Pawinskiego St., Warsaw 02-106, Poland. Electronic address: bieganowski@imdik.pan.pl.) |
| Abstract | Hsp90 is an essential chaperone for more than 200 client proteins in eukaryotic cells. The human genome encodes two highly similar cytosolic Hsp90 proteins called Hsp90α and Hsp90β. Most of the client proteins can interact with either Hsp90 protein; however, only a handful client proteins and one co-chaperone that interact specifically with one of the Hsp90 isoforms were identified. Structural differences underlying these isoform-specific interactions were not studied. Here we report for the first time that the Hsp90 co-chaperone Aha1 interacts preferentially with Hsp90α. The distinction depends on the middle domain of Hsp90. The middle domain of Hsp90α is also responsible for the slow growth phenotype of yeasts that express this isoform as a sole source of Hsp90. These results suggest that differences in the middle domain of Hsp90α and Hsp90β may be responsible for the isoform-specific interactions with selected proteins. Also shown here within, we determine that preferential chaperoning of cIAP1 by Hsp90β is mediated by the N-terminal domain of this isoform. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 2 |
| Volume Number | 1853 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-02-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | HSP90 Heat-Shock Proteins Chemistry Metabolism Molecular Chaperones Saccharomyces Cerevisiae HEK293 Cells Inhibitor Of Apoptosis Proteins Mutation Genetics Protein Binding Protein Isoforms Protein Multimerization Protein Structure, Tertiary Saccharomyces Cerevisiae Proteins Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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