Molecular basis for dissimilar nuclear trafficking of the actin-bundling protein isoforms T- and L-plastin |
| |
Authors: | Delanote Veerle Van Impe Katrien De Corte Veerle Bruyneel Erik Vetter Guillaume Boucherie Ciska Mareel Marc Vandekerckhove Joël Friederich Evelyne Gettemans Jan |
| |
Institution: | Department of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB), Ghent University, A. Baertsoenkaai 3, B-9000, Ghent, Belgium. |
| |
Abstract: | 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. |
| |
Keywords: | actin-binding protein collagen invasion CRM1 fimbrin nuclear export sequence plastin |
本文献已被 PubMed 等数据库收录! |
|