Reference : Molecular basis for dissimilar nuclear trafficking of the actin-bundling protein isof...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Molecular basis for dissimilar nuclear trafficking of the actin-bundling protein isoforms T- and L-plastin.
Delanote, Veerle [> >]
Van Impe, Katrien [> >]
De Corte, Veerle [> >]
Bruyneel, Erik [> >]
Vetter, Guillaume [> >]
Boucherie, Ciska [> >]
Mareel, Marc [> >]
Vandekerckhove, Joel [> >]
Friederich, Evelyne mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Gettemans, Jan [> >]
Traffic (Copenhagen, Denmark)
Yes (verified by ORBilu)
[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.

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