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dc.contributor.authorJul-Larsen, Åsneeng
dc.contributor.authorGrudic, Amraeng
dc.contributor.authorBjerkvig, Rolfeng
dc.contributor.authorBøe, Stig O.eng
dc.date.accessioned2011-04-08T07:43:07Z
dc.date.available2011-04-08T07:43:07Z
dc.date.issued2010-11-21eng
dc.identifier.citationBMC Molecular Biology 11:89en_US
dc.identifier.issn1471-2199eng
dc.identifier.urihttp://hdl.handle.net/1956/4639
dc.description.abstractBackground The promyelocytic leukemia (PML) protein participates in a number of cellular processes, including transcription regulation, apoptosis, differentiation, virus defense and genome maintenance. This protein is structurally organized into a tripartite motif (TRIM) at its N-terminus, a nuclear localization signal (NLS) at its central region and a C-terminus that varies between alternatively spliced isoforms. Most PML splice variants target the nucleus where they define sub-nuclear compartments termed PML nuclear bodies (PML NBs). However, PML variants that lack the NLS are also expressed, suggesting the existence of PML isoforms with cytoplasmic functions. In the present study we expressed PML isoforms with a mutated NLS in U2OS cells to identify potential cytoplasmic compartments targeted by this protein. Results Expression of NLS mutated PML isoforms in U2OS cells revealed that PML I targets early endosomes, PML II targets the inner nuclear membrane (partially due to an extra NLS at its C-terminus), and PML III, IV and V target late endosomes/lysosomes. Clustering of PML at all of these subcellular locations depended on a functional TRIM domain. Conclusions This study demonstrates the capacity of PML to form macromolecular protein assemblies at several different subcellular sites. Further, it emphasizes a role of the variable C-terminus in subcellular target selection and a general role of the N-terminal TRIM domain in promoting protein clustering.en_US
dc.language.isoengeng
dc.publisherBioMed Centraleng
dc.rightsAttribution CC BYeng
dc.rights.urihttp://creativecommons.org/licenses/by/2.0eng
dc.titleSubcellular distribution of nuclear import-defective isoforms of the promyelocytic leukemia proteineng
dc.typePeer reviewedeng
dc.typeJournal articleeng
dc.subject.nsiVDP::Medical disciplines: 700eng
dc.rights.holderCopyright 2010 Jul-Larsen et al; licensee BioMed Central Ltd.
dc.rights.holderJul-Larsen et al.eng
dc.type.versionpublishedVersioneng
bora.peerreviewedPeer reviewedeng
bora.cristinID526672eng
bibo.doihttp://dx.doi.org/10.1186/1471-2199-11-89eng
dc.identifier.cristinID526672eng
dc.identifier.doihttp://dx.doi.org/10.1186/1471-2199-11-89


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