Reference : Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promo...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/6269
Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells
English
Janji, B. [Laboratory for Molecular Biology, Genomics and Modelling, Public Research Centre for Health (CRP-Santé), 84 Val Fleuri, 1526 Luxembourg, Luxembourg]
Giganti, A. [Laboratory for Molecular Biology, Genomics and Modelling, Public Research Centre for Health (CRP-Santé), 84 Val Fleuri, 1526 Luxembourg, Luxembourg]
De Corte, V. [Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Albert Baertsoenkaai 3, 9000 Ghent, Belgium, Flanders Interuniversity, Institute for Biotechnology (V.I.B.), 9052 Ghent, Belgium]
Catillon, M. [Laboratory for Molecular Biology, Genomics and Modelling, Public Research Centre for Health (CRP-Santé), 84 Val Fleuri, 1526 Luxembourg, Luxembourg]
Bruyneel, E. [Laboratory of Experimental Cancerology, Department of Radiotherapy and Nuclear Medicine, Ghent University Hospital (1P7), De Pintelaan 185, 9000 Ghent, Belgium]
Lentz, D. [Laboratory for Molecular Biology, Genomics and Modelling, Public Research Centre for Health (CRP-Santé), 84 Val Fleuri, 1526 Luxembourg, Luxembourg]
Plastino, J. [Laboratoire Physicochimie Curie, UMR168 CNRS, Institut Curie, 11 rue Pierre et Marie Curie, 75231 Paris Cedex 05, France]
Gettemans, J. [Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Albert Baertsoenkaai 3, 9000 Ghent, Belgium, Flanders Interuniversity, Institute for Biotechnology (V.I.B.), 9052 Ghent, Belgium]
Friederich, Evelyne mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
2006
Journal of Cell Science
Company of Biologists
119
9
1947-1960
Yes (verified by ORBilu)
International
0021-9533
1477-9137
Cambridge
United Kingdom
[en] Actin bundling ; CH-domain ; Fimbrin ; Invasion ; Motility ; F actin ; L plastin protein ; Vero cell ; Actins ; Amino Acid Sequence ; Animals ; Cell Line ; Cercopithecus aethiops ; Cytoskeleton ; Humans ; Microfilament Proteins ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Protein Binding ; Serine ; Animalia
[en] L-plastin, a malignant transformation-associated protein, is a member of a large family of actin filament cross-linkers. Here, we analysed how phosphorylation of L-plastin on Ser5 of the headpiece domain regulates its intracellular distribution and its interaction with F-actin in transfected cells and in in vitro assays. Phosphorylated wild-type L-plastin localised to the actin cytoskeleton in transfected Vero cells. Ser5Ala substitution reduced the capacity of L-plastin to localise with peripheral actin-rich membrane protrusions. Conversely, a Ser5Glu variant mimicking a constitutively phosphorylated state, accumulated in actin-rich regions and promoted the formation of F-actin microspikes in two cell lines. Similar to phosphorylated wild-type L-plastin, this variant remained associated with cellular F-actin in detergent-treated cells, whereas the Ser5Ala variant was almost completely extracted. When compared with non-phosphorylated protein, phosphorylated L-plastin and the Ser5Glu variant bound F-actin more efficiently in an in vitro assay. Importantly, expression of L-plastin elicited collagen invasion in HEK293T cells, in a manner dependent on Ser5 phosphorylation. Based on our findings, we propose that conversely to other calponin homology (CH)-domain family members, phosphorylation of L-plastin switches the protein from a low-activity to a high-activity state. Phosphorylated L-plastin might act as an integrator of signals controlling the assembly of the actin cytoskeleton and cell motility in a 3D-space.
http://hdl.handle.net/10993/6269
10.1242/jcs.02874

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