Linked Life Data

15215316

Source:http://linkedlifedata.com/resource/pubmed/id/15215316

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2004-8-27
pubmed:abstractText
The CHIP ubiquitin ligase turns molecular chaperones into protein degradation factors. CHIP associates with the chaperones Hsc70 and Hsp90 during the regulation of signaling pathways and during protein quality control, and directs chaperone-bound clients to the proteasome for degradation. Obviously, this destructive activity should be carefully controlled. Here, we identify the cochaperone HspBP1 as an inhibitor of CHIP. HspBP1 attenuates the ubiquitin ligase activity of CHIP when complexed with Hsc70. As a consequence, HspBP1 interferes with the CHIP-induced degradation of immature forms of the cystic fibrosis transmembrane conductance regulator (CFTR) and stimulates CFTR maturation. Our data reveal a novel regulatory mechanism that determines folding and degradation activities of molecular chaperones.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-10075921, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-10330192, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-10330337, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-10671488, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11146632, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11146634, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11222862, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11395418, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11557750, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11600451, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11676916, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11743028, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-11884745, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-12069690, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-12239347, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-12297498, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-12417338, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-12559985, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-12743025, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-12832480, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-14507928, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-14508491, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-14526102, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-14532117, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-2808522, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-6656655, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-7553863, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-7553864, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-7692448, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-8557666, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-9188468, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-9321400, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-9325249, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-9830037, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-9843494, http://linkedlifedata.com/resource/pubmed/commentcorrection/15215316-9922380
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/CFTR protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cystic Fibrosis Transmembrane..., http://linkedlifedata.com/resource/pubmed/chemical/HSC70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSPA8 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/HSPBP1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/STUB1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1059-1524
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4003-10
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.
pubmed:affiliation
Institut für Zellbiologie and Bonner Forum Biomedizin, Rheinische Friedrich-Wilhelms-Universität Bonn, D-53121 Bonn, Germany.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't