Regulation of myosin light chain phosphorylation by RhoB in neuronal cells

Conway, A.M., James, A.B. , O'Kane, E.M., Rakhit, S. and Morris, B.J. (2004) Regulation of myosin light chain phosphorylation by RhoB in neuronal cells. Experimental Cell Research, 300, pp. 35-42. (doi:10.1016/j.yexcr.2004.06.022)

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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 R

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:James, Dr Allan
Authors: Conway, A.M., James, A.B., O'Kane, E.M., Rakhit, S., and Morris, B.J.
College/School:College of Medical Veterinary and Life Sciences > Institute of Neuroscience and Psychology
College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Experimental Cell Research
Publisher:Elsevier
ISSN:0014-4827
ISSN (Online):1090-2422
Published Online:01 January 2004

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