分子伴護子(Molecularchaperones) ，即所謂的熱休克蛋白(Heatshock proteins) ，此類蛋白質會幫助維持哺乳類細胞之恆定性。熱休克蛋白可藉由與不同分子量的分子伴護子做用，促使ATP協助保護蛋白質(clientproteins)之結構改變，進而調控細胞間的重要訊息傳導路徑。許多熱休克 蛋白的保護蛋白在人類癌症發展過程中發揮關鍵作用，因此以熱休克蛋白為標的之抗癌治療持續在發展。人類Tidl蛋白質是DnaJ分子伴護子家族的一員，具有腫瘤抑制功能，可藉由促使致癌激晦泛素化而被裂解。目前我們研究結果指出:Tidl會參與調控Erbs致癌家族的相關訊息傳導，達 到抗腫瘤的功能。因此本文章將討論我們在乳腺癌、頭頸癌及肺腺癌中Tidl的表現及抗腫瘤功能上的新發現。此外，運用Tidl做為熱休克蛋白標的之抗癌治療也將加以探討。

Molecular chaperones, commonly known as heat shock proteins (HSPs), are essential for mammalian cells to maintain homeostasis. HSPs may interact with diverse co-chaperones to induce an ATPase-coupled structural change in the client proteins and to regulate critical signaling networks. Many HSP client proteins are known to play a key role in human cancers, and strategy targeting HSP has been developed as an important approach for therapeutic application in human cancers. The human tumorous imaginal disc 1 (Tid1) protein, a DnaJ co-chaperone, is a tumor suppressor and is known to promote ubiquitin-mediated degradation of oncogenic kinases. Recent studies from our group have shown that Tid1 functions as a tumor suppressor through affecting ErbB-related signaling. In this article, the recent findings on the function and expression of Tid1 in breast cancer, head and neck cancer, and lung adenocarcinoma will be reviewed. In addition, the potential application of Tid1 as a novel target for HSP directed therapy will be discussed.