BORA - UiB

Bergen Open Research Archive

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

Bergen Open Research Archive

Show simple item record

dc.contributor.author Jul-Larsen, Åsne
dc.contributor.author Grudic, Amra
dc.contributor.author Bjerkvig, Rolf
dc.contributor.author Bøe, Stig O.
dc.date.accessioned 2011-04-08T07:43:07Z
dc.date.available 2011-04-08T07:43:07Z
dc.date.issued 2010-11-21
dc.identifier.citation BMC Molecular Biology 11:89 en_US
dc.identifier.issn 1471-2199
dc.identifier.uri http://dx.doi.org/10.1186/1471-2199-11-89
dc.identifier.uri http://hdl.handle.net/1956/4639
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 en_US
dc.publisher BioMed Central en
dc.rights Copyright 2010 Jul-Larsen et al; licensee BioMed Central Ltd. en_US
dc.rights.uri http://creativecommons.org/licenses/by/2.0 en_US
dc.title Subcellular distribution of nuclear import-defective isoforms of the promyelocytic leukemia protein en_US
dc.type Peer reviewed en
dc.type Journal article en
dc.subject.nsi VDP::Medical disciplines: 700 en_US
dc.rightsHolder Jul-Larsen et al. en_US
dc.type.version publishedVersion en_US
bora.cristinID 526672


Files in this item

 

This item appears in the following Collection(s)

Show simple item record

Copyright 2010 Jul-Larsen et al; licensee BioMed Central Ltd. Except where otherwise noted, this item's license is described as Copyright 2010 Jul-Larsen et al; licensee BioMed Central Ltd.

Search BORA


Browse

My Account