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Vol. 12, Issue 10, 3060-3073, October 2001
Department of Pathology, Helsinki University Hospital, and
Neuroscience Program, Biomedicum, University of Helsinki, FIN-00014
Helsinki, Finland
Actin-containing microfilaments control cell shape, adhesion, and
contraction. In striated muscle, 
-actinin and other Z-disk proteins
coordinate the organization and functions of actin filaments. In smooth
muscle and nonmuscle cells, periodic structures termed dense bodies and
dense regions, respectively, are thought to serve functions analogous
to Z-discs. We describe here identification and characterization of
human palladin, a protein expressed mainly in smooth muscle and
nonmuscle and distributed along microfilaments in a periodic manner
consistent with dense regions/bodies. Palladin contains three
Ig-domains most homologous to the sarcomeric Z-disk protein myotilin.
The N terminus includes an FPPPP motif recognized by the Ena-Vasp
homology domain 1 domain in Ena/vasodilatator-stimulated phosphoprotein (VASP)/Wiscott-Aldrich syndrome protein (WASP) protein
family. Cytoskeletal proteins with FPPPP motif target Ena/VASP/WASP
proteins to sites of actin modulation. We identified palladin in a
yeast two-hybrid search as an ezrin-associated protein. An interaction
between palladin and ezrin was further verified by affinity
precipitation and blot overlay assays. The interaction was mediated by
the -helical domain of ezrin and by Ig-domains 2-3 of palladin.
Ezrin is typically a component of the cortical cytoskeleton, but in
smooth muscle cells it is localized along microfilaments. These cells
express palladin abundantly and thus palladin may be involved in the
microfilament localization of ezrin. Palladin expression was
up-regulated in differentiating dendritic cells (DCs), coinciding with
major cytoskeletal and morphological alterations. In immature DCs,
palladin localized in actin-containing podosomes and in mature DCs
along actin filaments. The regulated expression and localization
suggest a role for palladin in the assembly of DC cytoskeleton.
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