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TitlePlakophilin-3 Binds the Membrane and Filamentous Actin without Bundling F-Actin.
Journal, issue, pagesInt J Mol Sci, Vol. 24, Issue 11, Year 2023
Publish dateMay 29, 2023
AuthorsJyoti Gupta / Erumbi S Rangarajan / Regina B Troyanovsky / Indrajyoti Indra / Sergey M Troyanovsky / Tina Izard /
PubMed AbstractPlakophilin-3 is a ubiquitously expressed protein found widely in epithelial cells and is a critical component of desmosomes. The plakophilin-3 carboxy-terminal domain harbors nine armadillo repeat ...Plakophilin-3 is a ubiquitously expressed protein found widely in epithelial cells and is a critical component of desmosomes. The plakophilin-3 carboxy-terminal domain harbors nine armadillo repeat motifs with largely unknown functions. Here, we report the 5 Å cryogenic electron microscopy (cryoEM) structure of the armadillo repeat motif domain of plakophilin-3, one of the smaller cryoEM structures reported to date. We find that this domain is a monomer or homodimer in solution. In addition, using an in vitro actin co-sedimentation assay, we show that the armadillo repeat domain of plakophilin-3 directly interacts with F-actin. This feature, through direct interactions with actin filaments, could be responsible for the observed association of extra-desmosomal plakophilin-3 with the actin cytoskeleton directly attached to the adherens junctions in A431 epithelial cells. Further, we demonstrate, through lipid binding analyses, that plakophilin-3 can effectively be recruited to the plasma membrane through phosphatidylinositol-4,5-bisphosphate-mediated interactions. Collectively, we report on novel properties of plakophilin-3, which may be conserved throughout the plakophilin protein family and may be behind the roles of these proteins in cell-cell adhesion.
External linksInt J Mol Sci / PubMed:37298410 / PubMed Central
MethodsEM (single particle)
Resolution5.03 Å
Structure data

EMDB-40675: Cryogenic electron microscopy map of human plakophilin-3
Method: EM (single particle) / Resolution: 5.03 Å

Source
  • Homo sapiens (human)

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