Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-12-14
pubmed:abstractText
Ubiquitination regulates important cellular processes, including the DNA damage response (DDR) and DNA repair. The complexity of the ubiquitin-mediated signals is decoded by ubiquitin receptors, which contain protein modules named ubiquitin binding domains (UBDs). We previously identified a new ubiquitin ligase, RNF168, involved in DDR and endowed with two UBDs named MIU (motif interacting with ubiquitin). Here we have provided the identification of a novel UBD, the UMI (UIM- and MIU-related UBD), present in RNF168, and characterized the interaction surface with ubiquitin, centered on two Leu residues. We have demonstrated that integrity of the UMI, in addition to the MIUs, is necessary for the proper localization of RNF168 and for ubiquitination of nuclear proteins, including histone H2A. Finally, we have shown that simultaneous inactivation of UMI and MIUs prevents the recruitment to DDR foci of the crucial downstream mediator 53BP1.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-10477747, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-11395416, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-11919637, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-12226657, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-16064137, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-16499958, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-17013377, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-17034365, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-17355622, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-17525341, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-17525342, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-18001824, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-18001825, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-18006705, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-18077395, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-18082599, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-18724939, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19007773, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19203578, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19203579, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19217402, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19325622, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19325626, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19500350, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19754430, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19773779, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-19948475, http://linkedlifedata.com/resource/pubmed/commentcorrection/21041483-20541996
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1098-5549
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
118-26
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed-meshheading:21041483-Amino Acid Sequence, pubmed-meshheading:21041483-Base Sequence, pubmed-meshheading:21041483-Binding Sites, pubmed-meshheading:21041483-Cell Line, pubmed-meshheading:21041483-DNA Damage, pubmed-meshheading:21041483-DNA Primers, pubmed-meshheading:21041483-DNA Repair, pubmed-meshheading:21041483-Histones, pubmed-meshheading:21041483-Humans, pubmed-meshheading:21041483-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:21041483-Leucine, pubmed-meshheading:21041483-Molecular Sequence Data, pubmed-meshheading:21041483-Mutant Proteins, pubmed-meshheading:21041483-Nuclear Proteins, pubmed-meshheading:21041483-Protein Binding, pubmed-meshheading:21041483-Protein Structure, Tertiary, pubmed-meshheading:21041483-Recombinant Fusion Proteins, pubmed-meshheading:21041483-Sequence Homology, Amino Acid, pubmed-meshheading:21041483-Signal Transduction, pubmed-meshheading:21041483-Ubiquitin, pubmed-meshheading:21041483-Ubiquitin-Protein Ligases, pubmed-meshheading:21041483-Ubiquitination
pubmed:year
2011
pubmed:articleTitle
UMI, a novel RNF168 ubiquitin binding domain involved in the DNA damage signaling pathway.
pubmed:affiliation
Department of DISCAFF and DFB Center, University of Piemonte Orientale A. Avogadro, 28100 Novara, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't