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Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells
Janji, B.; Giganti, A.; De Corte, V. et al.
2006In Journal of Cell Science, 119 (9), p. 1947-1960
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Keywords :
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
Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
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 ;  University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Language :
English
Title :
Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells
Publication date :
2006
Journal title :
Journal of Cell Science
ISSN :
1477-9137
Publisher :
Company of Biologists, Cambridge, United Kingdom
Volume :
119
Issue :
9
Pages :
1947-1960
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBilu :
since 18 September 2013

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