tailieunhanh - Báo cáo khoa học: The proline-rich protein palladin is a binding partner for profilin

Palladin is an actin-associated protein that has been suggested to play crit-ical roles in establishing cell morphology and maintaining cytoskeletal organization in a wide variety of cell types. Palladin has been shown previ-ously to bind directly to three different actin-binding proteins vasodilator-stimulated phosphoprotein (VASP), a-actinin and ezrin, suggesting that it functions as an organizing unit that recruits actin-regulatory proteins to specific subcellular sites. | iFEBS Journal The proline-rich protein palladin is a binding partner for profilin Malika Boukhelifa1 Monica Moza2 Thomas Johansson3 Andrew Rachlin1 Mana Parast1 Stefan Huttelmaier4 Partha Roy5 Brigitte M Jockusch4 Olli Carpen2 6 Roger Karlsson3 and Carol A Otey1 1 Department of Celland Molecular Physiology and Neuroscience Center University of North Carolina at Chapel Hill USA 2 Biomedicum Neuroscience Program and Department of Pathology University of Helsinki Finland 3 Department of Cell Biology Wenner Gren Institute Stockholm University Sweden 4 Cell Biology ZoologicalInstitute TechnicalUniversity of Braunschweig Germany 5 Bioengineering Department University of Pittsburgh USA 6 Department of Pathology University of Turku and Turku University Central Hospital Finland Keywords Actin assembly Ena Mena VASP lamellipodium migration Correspondence C. A. Otey. CB 7545 Department of Cell and Molecular Physiology UNCH Chapel Hill NC 27599-7545 USA Fax 919 966 6927 Tel. 919 966 8239 E-mail carol_otey@ The first three authors contributed equally to this work. Received 26 September 2005 accepted 27 October 2005 Palladin is an actin-associated protein that has been suggested to play critical roles in establishing cell morphology and maintaining cytoskeletal organization in a wide variety of cell types. Palladin has been shown previously to bind directly to three different actin-binding proteins vasodilator-stimulated phosphoprotein VASP a-actinin and ezrin suggesting that it functions as an organizing unit that recruits actin-regulatory proteins to specific subcellular sites. Palladin contains sequences resembling a motif known to bind profilin. Here we demonstrate that palladin is a binding partner for profilin interacting with profilin via a poly proline-containing sequence in the amino-terminal half of palladin. Double-label immunofluorescence staining shows that palladin and profilin partially colocalize in actin-rich structures in cultured astrocytes. Our .