The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry

The Hsp70/Hsp90 chaperone cycles depend on the coordinated interplay of several co-chaperones including Hsp40, Hop and peptidyl-prolyl isomerases such as FKBP52. Because of the many proteins involved in these interactions it is often difficult to delineate all possible combinations of subunits in th...

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Detalles Bibliográficos
Autores principales: Schmidt, Carla, Beilsten-Edmands, Victoria, Robinson, Carol V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2015
Materias:
Research Perspective
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4621890/
https://www.ncbi.nlm.nih.gov/pubmed/26286954
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author Schmidt, Carla
Beilsten-Edmands, Victoria
Robinson, Carol V.
author_facet Schmidt, Carla
Beilsten-Edmands, Victoria
Robinson, Carol V.
author_sort Schmidt, Carla
collection PubMed
description The Hsp70/Hsp90 chaperone cycles depend on the coordinated interplay of several co-chaperones including Hsp40, Hop and peptidyl-prolyl isomerases such as FKBP52. Because of the many proteins involved in these interactions it is often difficult to delineate all possible combinations of subunits in the complexes formed. We employed mass spectrometry to monitor the assembly and to determine the favoured pathways within these chaperone cycles. Combining the subunit composition with chemical cross-linking and proteomics allowed us to define interaction interfaces, protein dynamics and new intermediates.
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spelling pubmed-46218902015-12-02 The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry Schmidt, Carla Beilsten-Edmands, Victoria Robinson, Carol V. Oncotarget Research Perspective The Hsp70/Hsp90 chaperone cycles depend on the coordinated interplay of several co-chaperones including Hsp40, Hop and peptidyl-prolyl isomerases such as FKBP52. Because of the many proteins involved in these interactions it is often difficult to delineate all possible combinations of subunits in the complexes formed. We employed mass spectrometry to monitor the assembly and to determine the favoured pathways within these chaperone cycles. Combining the subunit composition with chemical cross-linking and proteomics allowed us to define interaction interfaces, protein dynamics and new intermediates. Impact Journals LLC 2015-07-22 /pmc/articles/PMC4621890/ /pubmed/26286954 Text en Copyright: © 2015 Schmidt et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Perspective
Schmidt, Carla
Beilsten-Edmands, Victoria
Robinson, Carol V.
The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry
title The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry
title_full The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry
title_fullStr The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry
title_full_unstemmed The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry
title_short The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry
title_sort joining of the hsp90 and hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry
topic Research Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4621890/
https://www.ncbi.nlm.nih.gov/pubmed/26286954
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