title: The proline-rich protein palladin is a binding partner for profilin.
abstract: 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), alpha-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 results suggest that palladin may play an important role in recruiting profilin to sites of actin dynamics.
authors.affiliation: Department of Cell and Molecular Physiology and Neuroscience Center, University of North Carolina at Chapel Hill, 27599-7545, USA.
authors.forename: Malika
authors.initials: M
authors.lastname: Boukhelifa
authors.forename: Monica
authors.initials: M
authors.lastname: Moza
authors.forename: Thomas
authors.initials: T
authors.lastname: Johansson
authors.forename: Andrew
authors.initials: A
authors.lastname: Rachlin
authors.forename: Mana
authors.initials: M
authors.lastname: Parast
authors.forename: Stefan
authors.initials: S
authors.lastname: Huttelmaier
authors.forename: Partha
authors.initials: P
authors.lastname: Roy
authors.forename: Brigitte M
authors.initials: BM
authors.lastname: Jockusch
authors.forename: Olli
authors.initials: O
authors.lastname: Carpen
authors.forename: Roger
authors.initials: R
authors.lastname: Karlsson
authors.forename: Carol A
authors.initials: CA
authors.lastname: Otey
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D019556:COS Cells; D015815:Cell Adhesion Molecules / Q000378:metabolism; D002522:Chlorocebus aethiops; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D051379:Mice; D008840:Microfilament Proteins / Q000378:metabolism; D008957:Models, Genetic; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D051304:Profilins / Q000378:metabolism*; D011392:Proline / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D020349:Surface Plasmon Resonance / Q000379:methods; D041701:Swiss 3T3 Cells; D013997:Time Factors; D014162:Transfection; D000098662:Vasodilator-Stimulated Phosphoprotein
chemical_list: D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D008840:Microfilament Proteins; C412722:PALLD protein, human; D010750:Phosphoproteins; D051304:Profilins; D011994:Recombinant Proteins; C485873:palladin protein, mouse; D000098662:Vasodilator-Stimulated Phosphoprotein; D011392:Proline