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J. Biol. Chem., Vol. 281, Issue 11, 7406-7412, March 17, 2006

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Protein Interaction Analysis of ST14 Domains and Their Point and Deletion Mutants^*

Weiting Ge, Hanguang Hu, Kefeng Ding, Lifeng Sun, and Shu Zheng¹

From the College of Life Science, Zhejiang University, Hangzhou 310029, China and the Cancer Institute, Second Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou 310009, China

ST14 (suppression of tumorigenicity 14) is a transmembrane serine protease that contains a serine protease catalytic (SP) domain, an SEA domain, two complement subcomponent C1r/s (CUB) domains, and four low density lipoprotein receptor class A domains. Glutathione S-transferase fusion proteins with SP, CUB, and low density lipoprotein receptor domains and their corresponding mutants were generated to analyze protein interactions with these domains. Modified glutathione S-transferase pull-down assays demonstrated the interaction between the SP domain and hepatocyte growth factor activator inhibitor-1. With the same method, a CUB domain-interacting protein was isolated and turned out to be the transmembrane protein with epidermal growth factor-like and two follistatin-like 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-up-regulated 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 epidermal growth factor and CUB domains.

Received for publication, September 30, 2005 , and in revised form, January 9, 2005.

^* This work was supported by National Natural Science Foundation of China Grant 30200325 and National Basic Research Program of China Grant 2004CB518707. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 86-571-87784501; Fax: 86-571-87784404; E-mail: zhengshu{at}zju.edu.cn.

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