Protein interaction analysis of ST14 domains and their point and deletion mutants

doi:10.1074/jbc.M510687200

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Papers In Press, published online ahead of print January 9, 2006
J. Biol. Chem, 10.1074/jbc.M510687200
Submitted on September 30, 2005
Revised on January 9, 2006
Accepted on January 9, 2006

Protein interaction analysis of ST14 domains and their point and deletion mutants

Weiting Ge, Hanguang Hu, Kefeng Ding, Lifeng Sun, and Shu Zheng

Cancer Institute, Second Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou, Zhejiang 310009

Corresponding Author: waiting915{at}yahoo.com.cn

Suppression of tumorigenicity 14 (ST14) is a transmembrane serine protease that contains a serine protease catalytic (SP) domain, a SEA domain, two complement sub-component C1r/s (CUB) domains, and four low density lipoprotein receptor (LDLR) class A domains. GST fusion proteins with SP, CUB, LDLR domains, and their corresponding mutants were generated to analyze protein interactions with these domains. Modified GST pull down assays demonstrated the interaction between the SP domain and hepatocyte growth factor activator inhibitor-1 (HAI-1). With the same method, a CUB domain-interacting protein was isolated and turned out to be the transmembrane protein with an epidermal growth factor (EGF)-like domain and two kazal_1 domains 1 (TMEFF1). Quantitative real-time PCR revealed that the expression of the TMEFF1 gene was dependent on the transfection of the ST14 gene in the RKO cell line. Our results also suggested that ST14 and TMEFF1 were co-expressed in the human breast cancer cell line MCF7, human placenta, kidney, and liver tissues. Interestingly, these two genes were co-upregulated in kidney tumors versus normal tissues, consistent with our results that showed the dependence of TMEFF1 expression on ST14 in RKO cells. Finally, homology modeling studies suggested that TMEFF1 might form a complex with ST14 by an interaction between EGF and CUB domains.

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