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Subcellular distribution of nuclear import-defective isoforms of the promyelocytic leukemia protein

Bergen Open Research Archive

Show simple item record Jul-Larsen, Åsne eng Grudic, Amra eng Bjerkvig, Rolf eng Bøe, Stig O. eng 2011-04-08T07:43:07Z 2011-04-08T07:43:07Z 2010-11-21 eng
dc.identifier.citation BMC Molecular Biology 11:89 en_US
dc.identifier.issn 1471-2199 eng
dc.description.abstract Background 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.iso eng eng
dc.publisher BioMed Central eng
dc.rights Attribution CC BY eng
dc.rights.uri eng
dc.title Subcellular distribution of nuclear import-defective isoforms of the promyelocytic leukemia protein eng
dc.type Peer reviewed eng
dc.type Journal article eng
dc.subject.nsi VDP::Medical disciplines: 700 eng
dc.rights.holder Copyright 2010 Jul-Larsen et al; licensee BioMed Central Ltd.
dc.rights.holder Jul-Larsen et al. eng
dc.type.version publishedVersion eng
bora.peerreviewed Peer reviewed eng
bora.cristinID 526672 eng
bibo.doi eng
dc.identifier.cristinID 526672 eng

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