Dishevelled-1 Regulates Microtubule Stability: A New Function Mediated by Glycogen Synthase Kinase-3{beta}

doi:10.1083/jcb.151.1.83

Published online 3 October 2000. doi:10.1083/jcb.151.1.83

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© The Rockefeller University Press, 0021-9525/2000/10/83/ $5.00
The Journal of Cell Biology, Volume 151, Number 1, October 2, 2000 83-94

Original Article

Dishevelled-1 Regulates Microtubule Stability: A New Function Mediated by Glycogen Synthase Kinase-3ß

Olga Krylova^a,b, Marcus J. Messenger^a, and Patricia C. Salinas^a,b
^a The Randall Institute, King's College London, London, United Kingdom, WC2B 5RL
^b Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, United Kingdom, SW7 2AY

Correspondence to: Patricia C. Salinas, Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY. UK. Tel:44 020 7594 5208 Fax:44 020 7594 5207

Dishevelled has been implicated in the regulation of cell fatedecisions, cell polarity, and neuronal function. However, themechanism of Dishevelled action remains poorly understood. Herewe examine the cellular localization and function of the mouseDishevelled protein, DVL-1. Endogenous DVL-1 colocalizes withaxonal microtubules and sediments with brain microtubules. Expressionof DVL-1 protects stable microtubules from depolymerizationby nocodazole in both dividing cells and differentiated neuroblastomacells. Deletion analyses reveal that the PDZ domain, but notthe DEP domain, of DVL-1 is required for microtubule stabilization.The microtubule stabilizing function of DVL-1 is mimicked bylithium-mediated inhibition of glycogen synthase kinase-3ß(GSK-3ß) and blocked by expression of GSK-3ß. Thesefindings suggest that DVL-1, through GSK-3ß, can regulatemicrotubule dynamics. This new function of DVL-1 in controllingmicrotubule stability may have important implications for Dishevelledproteins in regulating cell polarity.

Key Words: WNT, granule cells, cerebellum, cytoskeleton, nocodazole

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