Phostensin是由KIAA 1949這個基因轉譯出來的,全長共有165個胺基酸,並且是第一型蛋白質磷酸水解酶的結合蛋白,在其胺基酸序列中有第一型蛋白質磷酸水解酶的結合模序(motif),且Phostensin會去結合F-actin的尖端(pointed end),進而調控肌動蛋白之動態平衡。先前實驗室已經證實Phostensin也會去結合Eps15 homology domain (EHD) protein,而EHD proteins已有文獻證實在細胞內囊胞輸送作用中扮演重要的角色,而大部分EHD結合蛋白質大部分都含有天門冬醯胺–脯胺酸–苯丙胺酸motif (NPF motif)可與EHD蛋白質的EH domain結合。但是Phostensin缺少NPF motif,也意味著EHD proteins與Phostensin此兩者之間是以不同以往的形式進行結合,在我的研究中,將去探討EHD proteins與Phostensin是如何進行結合,並鑑別兩者蛋白之間的相互作用,更進一步利用核磁共振的技術去研究兩者蛋白質結合的interaction domain之結構分析。
Phostensin, encoded by KIAA1949, is a protein phosphatase 1 (PP1)-binding protein. Phostensin also binds to the pointed ends of F-actin, modulating the actin dynamics. Previous studies in our laboratory have demonstrated that phostensin also binds to EHD proteins. EHD proteins play a critical role in regulation of endocytic transportation. Most of the EHD-binding proteins contain one Asp-Pro-Phe (NPF) motif that interacts with the EH domain of EHD proteins. However, phostensin lacks this NPF motif. In my study, I will extend the previous studies and identify how phostensin binds to EHD proteins, searching the interaction domains in both proteins and characterizing their interactions by NMR spectrometry.