English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/60961
Share/Impact:
Statistics
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

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

AuthorsKorczyński, J.; Krzemiński, Patryk
Issue Date2011
PublisherPolish Academy of Sciences
CitationActa Biochimica Polonica 58(1): 125-130 (2011)
AbstractInhibition 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.
URIhttp://hdl.handle.net/10261/60961
Identifiersissn: 0001-527X
Appears in Collections:(IBMCC) Artículos
Files in This Item:
File Description SizeFormat 
Is MLC phosphorylation.pdf1,72 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.