Is MLC phosphorylation essential for the recovery from ROCK inhibition in glioma C6 cells?

• Autorzy: Korczynski J. , Sobierajska K. , Krzeminski P. , Wasik A. , Wypych D. , Pomorski P. , Klopocka W.
• Języki publikacji: EN

Abstrakty

EN

Inhibition of Rho-associated protein kinase (ROCK) activity in glioma C6 cells induces changes in actin cytoskeleton organization and cell morphology similar to those observed in other types of cells with inhibited RhoA/ROCK signaling pathway. We show that phosphorylation of myosin light chains (MLC) induced by P2Y2 receptor stimulation in cells with blocked ROCK correlates in time with actin cytoskeleton reorganization, F-actin redistribution and stress fibers assembly followed by recovery of normal cell morphology. Presented results indicate that myosin light-chain kinase (MLCK) is responsible for the observed phosphorylation of MLC. We also found that the changes induced by P2Y2 stimulation in actin cytoskeleton dynamics and morphology of cells with inhibited ROCK, but not in the level of phosphorylated MLC, depend on the presence of calcium in the cell environment.

Słowa kluczowe

EN

actin; calcium signalling; myosin; myosin II; myosin light chain; phosphorylation; endoplasmic reticulum; saline; Rho-associated protein kinase; cell morphology

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2011
• Tom: 58
• Numer: 1
• Opis fizyczny: p.125-130,fig.,ref.

Twórcy

autor

Korczynski J.

• Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland

autor

Sobierajska K.

autor

Krzeminski P.

autor

Wasik A.

autor

Wypych D.

autor

Pomorski P.

autor

Klopocka W.

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