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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Boczek, Edgar E. Dehling, Marco Kaila, Ville R. I. Reefschläger, Lasse G. Seidl, Andreas Häusler, Elisabeth Buchner, Johannes Struller, Tobias J. |
| Description | Author Affiliation: Boczek EE ( Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany); Reefschläger LG ( Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany); Dehling M ( Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany); Struller TJ ( Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany); Häusler E ( Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany); Seidl A ( Sandoz Biopharmaceuticals, Hexal AG, 82041 Oberhaching, Germany.); Kaila VR ( Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany); Buchner J ( Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany); |
| Abstract | Hsp90 is a molecular chaperone involved in the activation of numerous client proteins, including many kinases. The most stringent kinase client is the oncogenic kinase v-Src. To elucidate how Hsp90 chaperones kinases, we reconstituted v-Src kinase chaperoning in vitro and show that its activation is ATP-dependent, with the cochaperone Cdc37 increasing the efficiency. Consistent with in vivo results, we find that Hsp90 does not influence the almost identical c-Src kinase. To explain these findings, we designed Src kinase chimeras that gradually transform c-Src into v-Src and show that their Hsp90 dependence correlates with compactness and folding cooperativity. Molecular dynamics simulations and hydrogen/deuterium exchange of Hsp90-dependent Src kinase variants further reveal increased transitions between inactive and active states and exposure of specific kinase regions. Thus, Hsp90 shifts an ensemble of conformations of v-Src toward high activity states that would otherwise be metastable and poorly populated. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 25 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-06-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | HSP90 Heat-Shock Proteins Metabolism Oncogene Protein Pp60(v-src) Animals Molecular Dynamics Simulation Chemistry Protein Conformation Recombinant Fusion Proteins Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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