Regulation of myosin light chain phosphorylation by RhoB in neuronal cells

Experimental Cell Research
A-M ConwayB J Morris

Abstract

The phosphorylation of myosin light chain (MLC) is a key regulatory point in the control of cellular morphology. Evidence suggests that RhoA-a member of the Rho GTPase family-regulates MLC phosphorylation via Rho kinase (ROK). Neurones display subtle alterations in their cytoarchitecture during the synaptic plasticity following high-frequency stimulation. We have recently demonstrated that RhoB, and not RhoA, is activated in neurones by high-frequency stimulation. However, the downstream consequences of RhoB activation in cells are unclear. In this study, we tested the hypothesis that RhoB might stimulate neuronal MLC phosphorylation. Transfection of PC12 cells with constitutively active RhoB increased MLC phosphorylation. Conversely, dominant-negative RhoB vectors reduced MLC phosphorylation. The effect of RhoB was attenuated by pretreatment with a selective ROK inhibitor. This confirms that Rho GTPases are important regulators of MLC phosphorylation, but suggests that, in neuronal cells, the control is exerted via RhoB rather than RhoA.

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Citations

Mar 7, 2014·Cell and Tissue Research·Lucie Duluc, Beata Wojciak-Stothard
Nov 22, 2011·The European Journal of Neuroscience·Sara BarberanBrian J Morris
May 19, 2010·Alcoholism, Clinical and Experimental Research·Traute Flatscher-BaderPeter A Wilce
Apr 23, 2013·Critical Reviews in Biochemistry and Molecular Biology·Alice V Schofield, Ora Bernard
Jan 12, 2011·Philosophical Transactions. Series A, Mathematical, Physical, and Engineering Sciences·Charles S Cockell

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