RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/25684577http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25684577http://www.w3.org/2000/01/rdf-schema#comment"The ubiquitin ligase CHIP plays an important role in cytosolic protein quality control by ubiquitinating proteins chaperoned by Hsp70/Hsc70 and Hsp90, thereby targeting such substrate proteins for degradation. We present a 2.91 Å resolution structure of the tetratricopeptide repeat (TPR) domain of CHIP in complex with the α-helical lid subdomain and unstructured tail of Hsc70. Surprisingly, the CHIP-TPR interacts with determinants within both the Hsc70-lid subdomain and the C-terminal PTIEEVD motif of the tail, exhibiting an atypical mode of interaction between chaperones and TPR domains. We demonstrate that the interaction between CHIP and the Hsc70-lid subdomain is required for proper ubiquitination of Hsp70/Hsc70 or Hsp70/Hsc70-bound substrate proteins. Posttranslational modifications of the Hsc70 lid and tail disrupt key contacts with the CHIP-TPR and may regulate CHIP-mediated ubiquitination. Our study shows how CHIP docks onto Hsp70/Hsc70 and defines a bipartite mode of interaction between TPR domains and their binding partners."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2015.01.003"xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Misra S."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Santarriaga S."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Scaglione K.M."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Nix J.C."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Stuehr D.J."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Amick J."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Chakravarti R."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Page R.C."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Dare M."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"McGlone C."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/author"Schlanger S."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/pages"472-482"xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/title"A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins."xsd:string
http://purl.uniprot.org/citations/25684577http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/25684577http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25684577
http://purl.uniprot.org/citations/25684577http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25684577
http://purl.uniprot.org/uniprot/#_P11142-mappedCitation-25684577http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25684577
http://purl.uniprot.org/uniprot/#_B3KTV0-mappedCitation-25684577http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25684577
http://purl.uniprot.org/uniprot/#_B4DTX2-mappedCitation-25684577http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25684577