|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
Pt 3
|
|
pubmed:dateCreated |
2010-2-4
|
|
pubmed:abstractText |
Promyelocytic leukemia nuclear bodies (PML-NBs) are mobile subnuclear organelles formed by PML and Sp100 protein. They have been reported to have a role in transcription, DNA replication and repair, telomere lengthening, cell cycle control and tumor suppression. We have conducted high-resolution 4Pi fluorescence laser-scanning microscopy studies complemented with correlative electron microscopy and investigations of the accessibility of the PML-NB subcompartment. During interphase PML-NBs adopt a spherical organization characterized by the assembly of PML and Sp100 proteins into patches within a 50- to 100-nm-thick shell. This spherical shell of PML and Sp100 imposes little constraint to the exchange of components between the PML-NB interior and the nucleoplasm. Post-translational SUMO modifications, telomere repeats and heterochromatin protein 1 were found to localize in characteristic patterns with respect to PML and Sp100. From our findings, we derived a model that explains how the three-dimensional organization of PML-NBs serves to concentrate different biological activities while allowing for an efficient exchange of components.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO-1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Small Ubiquitin-Related Modifier...,
http://linkedlifedata.com/resource/pubmed/chemical/Sp100 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
1477-9137
|
|
pubmed:author |
pubmed-author:ChungInnI,
pubmed-author:CremerChristophC,
pubmed-author:EngelhardtJohannJ,
pubmed-author:HellStefan WSW,
pubmed-author:HemmerichPeterP,
pubmed-author:JegouThibaudT,
pubmed-author:LangMarionM,
pubmed-author:MünchSandraS,
pubmed-author:RichterKarstenK,
pubmed-author:RippeKarstenK,
pubmed-author:UdvarhelyiAnikóA
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
1
|
|
pubmed:volume |
123
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
392-400
|
|
pubmed:meshHeading |
pubmed-meshheading:20130140-Antigens, Nuclear,
pubmed-meshheading:20130140-Autoantigens,
pubmed-meshheading:20130140-Cell Line, Tumor,
pubmed-meshheading:20130140-HeLa Cells,
pubmed-meshheading:20130140-Humans,
pubmed-meshheading:20130140-Intranuclear Inclusion Bodies,
pubmed-meshheading:20130140-Microscopy, Confocal,
pubmed-meshheading:20130140-Microscopy, Electron, Transmission,
pubmed-meshheading:20130140-Microscopy, Fluorescence,
pubmed-meshheading:20130140-Models, Biological,
pubmed-meshheading:20130140-Nuclear Proteins,
pubmed-meshheading:20130140-SUMO-1 Protein,
pubmed-meshheading:20130140-Small Ubiquitin-Related Modifier Proteins,
pubmed-meshheading:20130140-Transcription Factors,
pubmed-meshheading:20130140-Tumor Suppressor Proteins,
pubmed-meshheading:20130140-Ubiquitins
|
|
pubmed:year |
2010
|
|
pubmed:articleTitle |
Three-dimensional organization of promyelocytic leukemia nuclear bodies.
|
|
pubmed:affiliation |
Division of High Resolution Optical Microscopy, Deutsches Krebsforschungszentrum, 69120 Heidelberg, Germany.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
