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We previously showed that Dock3 forms a complex with Fyn and WASP (Wiskott\u2013Aldrich syndrome protein) family verprolin-homologous (WAVE) proteins at the plasma membrane, and subsequent Rac1 activation promotes actin polymerization. Here we show that Dock3 binds to and inactivates glycogen synthase kinase-3\u03b2 (GSK-3\u03b2) at the plasma membrane, thereby increasing the nonphosphorylated active form of collapsin response mediator protein-2 (CRMP-2), which promotes axon branching and microtubule assembly. Exogenously applied BDNF induced the phosphorylation of GSK-3\u03b2 and dephosphorylation of CRMP-2 in hippocampal neurons. Moreover, increased phosphorylation of GSK-3\u03b2 was detected in the regenerating axons of transgenic mice overexpressing Dock3 after optic nerve injury. These results suggest that Dock3 plays important roles downstream of BDNF signaling in the CNS, where it regulates cell polarity and promotes axonal outgrowth by stimulating dual pathways: actin polymerization and microtubule assembly.<\/jats:p>","DOI":"10.1523\/jneurosci.4884-11.2012","type":"journal-article","created":{"date-parts":[[2012,1,5]],"date-time":"2012-01-05T11:12:46Z","timestamp":1325761966000},"page":"264-274","source":"Crossref","is-referenced-by-count":74,"title":["Dock3 Stimulates Axonal Outgrowth via GSK-3\u03b2-Mediated Microtubule 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