Plakophilin 2: a critical scaffold for PKCalpha that regulates intercellular junction assembly

@article{citeulike:2802109, abstract = {Plakophilins (PKPs) are armadillo family members related to the classical cadherin-associated protein p120ctn. 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. 10.1083/jcb.200712133}, author = {Bass-Zubek, Amanda E. and Hobbs, Ryan P. and Amargo, Evangeline V. and Garcia, Nicholas J. and Hsieh, Sherry N. and Chen, Xinyu and Wahl, James K. and Denning, Mitchell F. and Green, Kathleen J. }, citeulike-article-id = {2802109}, doi = {http://dx.doi.org/10.1083/jcb.200712133}, journal = {J. Cell Biol.}, month = {May}, pages = {jcb.200712133+}, posted-at = {2008-06-28 23:00:53}, priority = {0}, title = {Plakophilin 2: a critical scaffold for PKC{alpha} that regulates intercellular junction assembly}, url = {http://dx.doi.org/10.1083/jcb.200712133}, year = {2008} }

TY - JOUR ID - citeulike:2802109 L3 - citeulike-article-id:2802109 TI - Plakophilin 2: a critical scaffold for PKC{alpha} that regulates intercellular junction assembly JF - J. Cell Biol. SP - jcb.200712133 N2 - Plakophilins (PKPs) are armadillo family members related to the classical cadherin-associated protein p120ctn. 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. 10.1083/jcb.200712133 AU - Bass-Zubek, Amanda AU - Hobbs, Ryan AU - Amargo, Evangeline AU - Garcia, Nicholas AU - Hsieh, Sherry AU - Chen, Xinyu AU - Wahl, James AU - Denning, Mitchell AU - Green, Kathleen PY - 2008/05/12/ UR - http://dx.doi.org/10.1083/jcb.200712133 ER -