| Autor: |
Bass-Zubek AE; Department of Pathology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA., Hobbs RP, Amargo EV, Garcia NJ, Hsieh SN, Chen X, Wahl JK 3rd, Denning MF, Green KJ |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of cell biology [J Cell Biol] 2008 May 19; Vol. 181 (4), pp. 605-13. Date of Electronic Publication: 2008 May 12. |
| DOI: |
10.1083/jcb.200712133 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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