Journal
JOURNAL OF CELL BIOLOGY
Volume 181, Issue 4, Pages 605-613Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200712133
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Funding
- NCI NIH HHS [R01CA122151, R01 CA122151, T32 CA009560, T32CA009560] Funding Source: Medline
- NIAMS NIH HHS [R01AR43380, R01 AR043380, R01AR41836, R01 AR041836] Funding Source: Medline
- NIDCR NIH HHS [R01 DE016905, 1R01DE016905] Funding Source: Medline
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Plakophilins (PKPs) are armadillo family members related to the classical cadherin-associated protein p120(ctn). PKPs localize to the cytoplasmic plaque of intercellular junctions and participate in linking the intermediate filament (IF)-binding protein desmoplakin (DP) to desmosomal cadherins. In response to cell-cell contact, PKP2 associates with DP in plaque precursors that form in the cytoplasm and translocate to nascent desmosomes. Here, we provide evidence that PKP2 governs DP assembly dynamics by scaffolding a DP-PKP2-protein kinase C alpha (PKC alpha) complex, which is disrupted by PKP2 knockdown. The behavior of a phosphorylation-deficient DP mutant that associates more tightly with IF is mimicked by PKP2 and PKC alpha knockdown and PKC pharmacological inhibition, all of which impair junction assembly. PKP2 knockdown is accompanied by increased phosphorylation of PKC substrates, raising the possibility that global alterations in PKC signaling may contribute to pathogenesis of congenital defects caused by PKP2 deficiency.
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