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Title: Identification and characterization of interacting protein of CD157
Keywords: CD157, proteasome, yeast two-hybrid, GST pull down, coimmunoprecipitation
Issue Date: 18-Aug-2004
Citation: NG SEOK SHIN (2004-08-18). Identification and characterization of interacting protein of CD157. ScholarBank@NUS Repository.
Abstract: CD157, a glycosyl phosphatidylinositol (GPI)- anchored glycoprotein expressed in both hematopoeitic and non-hematopoeitic cells, possesses ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities. CD157 has a receptor like function because cross-linking of CD157 with specific antibodies stimulates tyrosine phosphorylation and dephosphorylaion of selective proteins. Over-expression of CD157 in MCA102 cells results in tyrosine phosphorylation of focal adhesion kinase (FAK). However, the majority of signaling molecules that are involved in CD157 mediated tyrosine pathway are yet to be identified. Identifying the interacting partner(s) of CD157 may help to elucidate the function of CD157 in vivo and in vitro. Soluble CD157 was used as bait in yeast two-hybrid screening against Hela and B cell cDNA libraries. It was found that proteasome interacts with CD157, speculated a possible function of proteasome on the CD157. The specificity of the interaction of CD157 with proteasome has been investigated through GST pull down and coimmunoprecipitation study.
Appears in Collections:Master's Theses (Open)

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