| Reference : Molecular basis for dissimilar nuclear trafficking of the actin-bundling protein isof... |
| Scientific journals : Article | |||
| Life sciences : Biochemistry, biophysics & molecular biology | |||
| http://hdl.handle.net/10993/6275 | |||
| Molecular basis for dissimilar nuclear trafficking of the actin-bundling protein isoforms T- and L-plastin. | |
| English | |
| Delanote, Veerle [> >] | |
| Van Impe, Katrien [> >] | |
| De Corte, Veerle [> >] | |
| Bruyneel, Erik [> >] | |
| Vetter, Guillaume [> >] | |
| Boucherie, Ciska [> >] | |
| Mareel, Marc [> >] | |
| Vandekerckhove, Joel [> >] | |
Friederich, Evelyne  [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >] | |
| Gettemans, Jan [> >] | |
| 2005 | |
| Traffic (Copenhagen, Denmark) | |
| 6 | |
| 4 | |
| 335-45 | |
| Yes (verified by ORBilu) | |
| International | |
| 1398-9219 | |
| Denmark | |
| [en] Active Transport, Cell Nucleus ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Nucleus/drug effects/metabolism ; Cercopithecus aethiops ; Fatty Acids, Unsaturated/pharmacology ; Gene Products, rev/genetics/metabolism ; Humans ; Leucine/genetics/metabolism ; Membrane Glycoproteins ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Phenotype ; Phenylalanine/genetics/metabolism ; Phosphoproteins/genetics/metabolism ; Protein Isoforms/metabolism ; Protein Sorting Signals/drug effects ; Sequence Alignment | |
| [en] T- and L-plastin are highly similar actin-bundling proteins implicated in the regulation of cell morphology, lamellipodium protrusion, bacterial invasion and tumor progression. We show that T-plastin localizes predominantly to the cytoplasm, whereas L-plastin distributes between nucleus and cytoplasm in HeLa or Cos cells. T-plastin shows nuclear accumulation upon incubation of cells with the CRM1 antagonist leptomycin B (LMB). We identified a Rev-like nuclear export sequence (NES) in T-plastin that is able to export an otherwise nuclear protein in an LMB-dependent manner. Deletion of the NES promotes nuclear accumulation of T-plastin. Mutation of residues L17, F21 or L26 in the T-plastin NES inhibits nuclear efflux. L-plastin harbors a less conserved NES and lacks the F21 T-plastin residue. Insertion of a Phe residue in the L-plastin NES specifically enhances its export activity. These findings explain why both isoforms exhibit specific distribution patterns in eukaryotic cells. | |
| http://hdl.handle.net/10993/6275 |
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