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  • 學位論文

鑑定phostensin和EHD蛋白質之間的交互作用

Characterization of the interaction between EHD proteins and phostensin

指導教授 : 黃憲斌
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摘要


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。

並列摘要


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.

參考文獻


1.Cohen, P. (1989). "The structure and regulation of protein phosphatases." Annu Rev Biochem. 58: 453-508.
3.Blume-Jensen, P and T. Hunter (1995). "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification." FASEB J. 9: 576-596.
4.Taylor, S. S., E. Radzio-Andzelm and T. Hunter (1995). "How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase" FASEB J. 9: 1255-1266.
5.Dhanasekaran, N. (1998). " Cell signaling: an overview " Oncogen 17: 1329-1330.
7.Faux, M. C. & Scott, J. D. (1996) "More on target with protein phosphorylation: conferring specificity by location." Trends Biochem. Sci. 21, 312-315.

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