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Titolo:
Involvement of desmoplakin phosphorylation in the regulation of desmosomesby protein kinase C, in HeLa cells
Autore:
Amar, LS; Shabana, AM; Oboeuf, M; Martin, N; Forest, N;
Indirizzi:
UnivFrance 07, Lab Biol Odontol, Inst Biomed Cordeliers, F-75270 Paris 06,Univ Paris 07 Paris France 06 Inst Biomed Cordeliers, F-75270 Paris 06,
Titolo Testata:
CELL ADHESION AND COMMUNICATION
fascicolo: 2, volume: 7, anno: 1999,
pagine: 125 - 138
SICI:
1061-5385(1999)7:2<125:IODPIT>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
KIDNEY EPITHELIAL-CELLS; KERATIN INTERMEDIATE FILAMENTS; ADHESION MOLECULES; CARCINOMA-CELLS; INTERCELLULAR-ADHESION; CALCIUM-CONCENTRATION; PLAKOGLOBIN-BINDING; ADHERING JUNCTIONS; SPATIAL REGULATION; PLAQUE PROTEINS;
Keywords:
HeLa cells; desmoplakin; desmosome; protein kinase C; phosphorylation; TPA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Amar, LS Univage,15 07, Lab Biol Odontol, Inst Biomed Cordeliers, EscalierE,2eme Et Univ Paris 07 Escalier E,2eme Etage,15 Rue Ecole Med Paris France 06
Citazione:
L.S. Amar et al., "Involvement of desmoplakin phosphorylation in the regulation of desmosomesby protein kinase C, in HeLa cells", CELL AD COM, 7(2), 1999, pp. 125-138

Abstract

In the present study, we have examined how modulation of protein kinase C (PKC) activity affected desmosome organization in HeLa cells, Immunofluorescence and electron microscopy showed that PKC activation upon short exposure to 12-O-tetradecanoylphorbol 13-acetate (TPA) resulted in a reduction of intercellular contacts, splitting of desmosomes and dislocation of desmosomal components from the cell periphery towards the cytoplasm, As determined by immunoblot analysis of Triton X-100-soluble and -insoluble pools of proteins, these morphological changes were not correlated with modifications inthe extractability of both desmoglein and plakoglobin, but involved almostcomplete solubilization of the desmosomal plaque protein, desmoplakin, Immunoprecipitation experiments and immunoblotting with anti-phosphoserine, anti-phosphothreonine and anti-phosphotyrosine antibodies revealed that desmoplakin was mainly phosphorylated on serine and tyrosine residues in both treated and untreated cells. While phosphotyrosine content was not affected by PKC activation, phosphorylation on serine residues was increased by abouttwo-fold. This enhanced serine phosphorylation coincided with the increasein the protein solubility, suggesting that phosphorylation of desmoplakin may be a mechanism by which PKC mediates desmosome disassembly, Consistent with the loss of PKC activity, we also showed that down-modulation of the kinase (in response to prolonged TPA treatment) or its specific inhibition (by GF109203X) had opposite effects and increased desmosome formation, Takentogether, these results clearly demonstrate an important role for PKC in the regulation of desmosomal junctions in HeLa cells, and identify serine phosphorylation of desmoplakin as a crucial event in this pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 19:53:07