Ontology highlight
ABSTRACT:
SUBMITTER: Morgner N
PROVIDER: S-EPMC4431665 | biostudies-literature | 2015 May
REPOSITORIES: biostudies-literature
Morgner Nina N Schmidt Carla C Beilsten-Edmands Victoria V Ebong Ima-Obong IO Patel Nisha A NA Clerico Eugenia M EM Kirschke Elaine E Daturpalli Soumya S Jackson Sophie E SE Agard David D Robinson Carol V CV
Cell reports 20150423 5
Protein folding in cells is regulated by networks of chaperones, including the heat shock protein 70 (Hsp70) system, which consists of the Hsp40 cochaperone and a nucleotide exchange factor. Hsp40 mediates complex formation between Hsp70 and client proteins prior to interaction with Hsp90. We used mass spectrometry (MS) to monitor assemblies formed between eukaryotic Hsp90/Hsp70/Hsp40, Hop, p23, and a client protein, a fragment of the glucocorticoid receptor (GR). We found that Hsp40 promotes in ...[more]