Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2003-6-13
pubmed:abstractText
C-terminal-binding protein/brefeldin A-ADP ribosylated substrate (CtBP/BARS) plays key roles in development and oncogenesis as a transcription co-repressor, and in intracellular traffic as a promoter of Golgi membrane fission. Co-repressor activity is regulated by NAD(H) binding to CtBP/BARS, while membrane fission is associated with its acyl-CoA-dependent acyltransferase activity. Here, we report the crystal structures of rat CtBP/BARS in a binary complex with NAD(H), and in a ternary complex with a PIDLSKK peptide mimicking the consensus motif (PXDLS) recognized in CtBP/BARS cellular partners. The structural data show CtBP/BARS in a NAD(H)-bound dimeric form; the peptide binding maps the recognition site for DNA-binding proteins and histone deacetylases to an N-terminal region of the protein. The crystal structure together with the site-directed mutagenesis data and binding experiments suggest a rationale for the molecular mechanisms underlying the two fundamental co-existing, but diverse, activities supported by CtBP/BARS in the nucleus and in Golgi membranes.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-10089316, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-10089361, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-10364211, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-10369679, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-10586885, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-10592235, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-12037320, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-12419229, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-12429083, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-12530516, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-15299354, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-15299374, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-1758883, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-2025413, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-4737475, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-7479821, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-7624370, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-7719856, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-7984417, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-8114093, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-8120891, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-8302839, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-8440238, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-8580836, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-8692699, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-8740366, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-9126843, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-9144787, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-9353717, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-9382860, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-9724649, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805226-9757107
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3122-30
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:12805226-Acyl Coenzyme A, pubmed-meshheading:12805226-Amino Acid Sequence, pubmed-meshheading:12805226-Animals, pubmed-meshheading:12805226-Binding Sites, pubmed-meshheading:12805226-Carrier Proteins, pubmed-meshheading:12805226-Cell Membrane, pubmed-meshheading:12805226-Crystallography, X-Ray, pubmed-meshheading:12805226-Golgi Apparatus, pubmed-meshheading:12805226-Models, Molecular, pubmed-meshheading:12805226-Molecular Sequence Data, pubmed-meshheading:12805226-NAD, pubmed-meshheading:12805226-Peptides, pubmed-meshheading:12805226-Protein Binding, pubmed-meshheading:12805226-Protein Folding, pubmed-meshheading:12805226-Protein Structure, Tertiary, pubmed-meshheading:12805226-Rats, pubmed-meshheading:12805226-Recombinant Fusion Proteins, pubmed-meshheading:12805226-Repressor Proteins, pubmed-meshheading:12805226-Sequence Alignment, pubmed-meshheading:12805226-Transcription, Genetic, pubmed-meshheading:12805226-Transcription Factors
pubmed:year
2003
pubmed:articleTitle
CtBP/BARS: a dual-function protein involved in transcription co-repression and Golgi membrane fission.
pubmed:affiliation
Department of Physics-INFM, University of Genova, Via Dodecaneso 33, 16146 Genova, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't