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We showed previously that the PI3 kinase\u2013Akt pathway downstream of BDNF\/TrkB signaling stimulates synaptic delivery of PSD-95 via vesicular transport. However, vesicular transport requires PSD-95 palmitoylation to attach it to a lipid membrane. Also, PSD-95 insertion at synapses is known to require this lipid modification. Here, we show that BDNF\/TrkB signaling is also necessary for PSD-95 palmitoylation and its transport to synapses in mouse visual cortical layer 2\/3 neurons. However, palmitoylation of PSD-95 requires the activation of another pathway downstream of BDNF\/TrkB, namely, signaling through phospholipase C\u03b3 and the brain-specific PKC variant protein kinase M \u03b6 (PKM\u03b6). We find that PKM\u03b6 selectively regulates phosphorylation of the palmitoylation enzyme ZDHHC8. Inhibition of PKM\u03b6 results in a reduction of synaptic PSD-95 accumulation<jats:italic>in vivo<\/jats:italic>, which can be rescued by overexpressing ZDHHC8. Therefore, TrkB and PKM\u03b6, two critical regulators of synaptic plasticity, facilitate PSD-95 targeting to synapses. These results also indicate that palmitoylation can be regulated by a trophic factor. Our findings have implications for neurodevelopmental disorders as well as aging brains.<\/jats:p>","DOI":"10.1523\/jneurosci.2190-11.2011","type":"journal-article","created":{"date-parts":[[2011,8,17]],"date-time":"2011-08-17T19:10:40Z","timestamp":1313608240000},"page":"11894-11904","source":"Crossref","is-referenced-by-count":68,"title":["TrkB and Protein Kinase M \u03b6 Regulate Synaptic Localization of PSD-95 in Developing 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