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

Jarosław Korczyński | Zendy; Katarzyna Sobierajska | Zendy; Patryk Krzemiński | Zendy; A. Wasik | Zendy; Dorota Wypych | Zendy; Paweł Pomorski | Zendy; Wanda Kłopocka | Zendy

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

Author(s) -

Jarosław Korczyński,

Katarzyna Sobierajska,

Patryk Krzemiński,

A. Wasik,

Dorota Wypych,

Paweł Pomorski,

Wanda Kłopocka

Publication year - 2011

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2011_2295

Subject(s) - myosin light chain kinase , rhoa , microbiology and biotechnology , cytoskeleton , rho associated protein kinase , actin , phosphorylation , actin cytoskeleton , myosin , chemistry , biology , signal transduction , cell , biochemistry

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.

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