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Published online 24 July 2006. doi:10.1083/jcb.200511028
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 3, 415-424
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Article

 Requirement of dendritic Akt degradation by the ubiquitin–proteasome system for neuronal polarity

Dong Yan1,2, Li Guo1,2, and Yizheng Wang1,2

1 Laboratory of Neural Signal Transduction, Institute of Neuroscience, Shanghai Institutes of Biological Sciences, and 2 Key Laboratory of Neurobiology, The Graduate School, Chinese Academy of Science, Shanghai 200031, China

Correspondence to Y.Z. Wang: yzwang{at}ion.ac.cn

Asymmetric distributions of activities of the protein kinases Akt and glycogen synthase kinase 3ß (GSK-3ß) are critical for the formation of neuronal polarity. However, the mechanisms underlying polarized regulation of this pathway remain unclear. In this study, we report that the instability of Akt regulated by the ubiquitin–proteasome system (UPS) is required for neuron polarity. Preferential distribution in the axons was observed for Akt but not for its target GSK-3ß. A photoactivatable GFP fused to Akt revealed the preferential instability of Akt in dendrites. Akt but not p110 or GSK-3ß was ubiquitinated. Suppressing the UPS led to the symmetric distribution of Akt and the formation of multiple axons. These results indicate that local protein degradation mediated by the UPS is important in determining neuronal polarity.

D. Yan and L. Guo contributed equally to this paper.

Abbreviations used in this paper: GSK-3ß, glycogen synthase kinase 3ß; myr, myristoyl; PA, photoactive; PI, phosphatidylinositol; Ub, ubiquitin; UPS, Ub–proteasome system; WT, wild type.


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