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The proline-rich protein palladin is a binding partner for profilin
Stockholm University, Faculty of Science, The Wenner-Gren Institute .
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2006 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 273, no 1, 26-33 p.Article in journal (Refereed) Published
Abstract [en]

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), α-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.

Place, publisher, year, edition, pages
2006. Vol. 273, no 1, 26-33 p.
Keyword [en]
Actin assembly Ena/Mena/VASP lamellipodium migration
National Category
Biological Sciences
URN: urn:nbn:se:su:diva-24628DOI: 10.1111/j.1742-4658.2005.05036.xOAI: diva2:197955
Part of urn:nbn:se:su:diva-727Available from: 2005-11-28 Created: 2005-11-28 Last updated: 2010-07-08Bibliographically approved
In thesis
1. Profilin:actin in cell motility: A search for profilin:actin binding proteins
Open this publication in new window or tab >>Profilin:actin in cell motility: A search for profilin:actin binding proteins
2005 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The profilin:actin complex is a major source of actin for actin filament growth in vivo. A number of proteins regulating either profilin or actin has been described since profilin:actin was isolated during the 1970s. Since then, profilin and actin and their binding partners have been intensively studied. The ability of profilin:actin to interact with the fast polymerizing end of actin filaments focus the interest to components that regulates this interaction; this is the theme in this thesis.

A chemically cross-linked and therefore non-dissociable profilin:actin complex, called PxA, was used in these studies which led to development of a rapid screening method to search for proteins that bind to profilin:actin. The method allows a simultaneous detection of proteins that separately interact with profilin, actin and/or profilin:actin. Here the technique was used to screen cell and tissue extracts, before and after gel filtration, for components that showed a unique interaction with the profilin:actin complex. Mass spectrometry was then used for their identification. Furthermore it was demonstrated that profilin:actin binding components are present in RNA containing, large molecular weight complexes.

Two different PxA immunizations generated two separate populations of affinity purified profilin and actin antibodies. The actin antibodies from these two populations showed significant differences in the staining pattern when used for fluorescence microscopy of tissue cultured cells. One of these appeared to bind monomeric actin while the other bound to filamentous actin. Both of the profilin antibody preparations stained cells in a dotted pattern. The distribution of epitopes recognized by the different actin antibody preparations was determined using a combination of protease digestion, gel electrophoresis and mass spectrometry. The result demonstrated partially different epitope recognition.

The actin associated protein palladin contains sequence motifs typical for profilin-binding proteins suggesting that profilin may bind palladin. The potential profilin-palladin interaction was studied using a combination of biochemical and histochemical techniques. The interaction was observed in vitro, and the two proteins co-distributed in actin rich regions in tissue cultured cells. These results suggest that palladin recruits profilin and/or profilin:actin to sites of actin dynamics.

Place, publisher, year, edition, pages
Stockholm: Wenner-Grens institut för experimentell biologi, 2005. 75 p.
profilin, actin
National Category
Cell Biology
urn:nbn:se:su:diva-727 (URN)91-7155-153-0 (ISBN)
Public defence
2005-12-19, De Geersalen, Geovetenskapens hus, Svante Arrhenius väg 8 A, Stockholm, 10:00
Available from: 2005-11-28 Created: 2005-11-28 Last updated: 2012-01-12Bibliographically approved

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