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

Jarosław Korczyński; Katarzyna Sobierajska; Patryk Krzemiński; Anna Wasik; Dorota Wypych; Paweł Pomorski; Wanda Kłopocka

doi:10.18388/abp.2011_2295

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

Jarosław Korczyński Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland.;
Katarzyna Sobierajska
Patryk Krzemiński
Anna Wasik
Dorota Wypych
Paweł Pomorski
Wanda Kłopocka

DOI: https://doi.org/10.18388/abp.2011_2295

Abstract

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.

Published

2011-03-07

Issue

Vol. 58 No. 1 (2011)

Section

Articles

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