由豬腦裡純化出來的後突觸質密區(postsynaptic density，簡稱PSD)結構相當緊密，使得研究PSD內部的結構組成相當不容易。本實驗室在之前發表的論文(Chang, 2007)裡發現CaMKIIα和α-tubulin在PSD裡會具有交互作用，而這兩種蛋白之間的關係在過去的研究文獻裡鮮少被提及。在這篇論文裡我們利用高濃度的urea將PSD打散後，再利用免疫吸附的方法來對PSD內部進行研究。由anti- CaMKIIα和anti-α-tubulin的免疫吸附結果可以知道CaMKIIα和α-tubulin這兩種蛋白質都會被吸附出來，確認了在PSD裡CaMKIIα和α-tubulin彼此之間是具有交互作用的；同時我們也發現actin、CaMKIIβ和β-tubulin會一同被吸附下來，顯示這幾種蛋白質在PSD裡可能會形成一個蛋白質複合體，我們在此將之稱為「C/T complex」。另外使用anti-β-tubulin antibodies進行免疫吸附同樣也可以將上述的幾種蛋白一起吸附下來，這也再次地說明了這些蛋白之間的確具有交互作用。透過了二次交叉免疫吸附的實驗，我們再次確認了這個以CaMKIIα和α、β-tubulin為主所組成的C/T complex的存在，同時也知道C/T complex可以快速地回復到原本的組成。我們進一步地利用化學交聯劑DTSP和對角線電泳的分析，確認在PSD裡CaMKIIα和α-tubulin是具有直接的交互作用，這兩種蛋白可直接被DTSP聯結成一個分子量約137 kDa的複合體，並且發現β-tubulin在PSD裡沒有和α-tubulin形成heterodimer。利用連續蔗糖濃度梯度，我們推測C/T complex並不是一個很巨大的物質。之後我們也使用cytosol來取代PSD作為研究的材料，發現C/T complex也有存在於cytosol裡，顯示C/T complex在細胞裡應該具有一定的功用。儘管目前我們對於C/T complex全部組成及存在於PSD和cytosol裡的功用是什麼尚不清楚，不過我們最後提出了一個假設的模型來說明C/T complex與CaMKIIα的localization之間可能的關係。

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