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J. Biol. Chem., Vol. 283, Issue 4, 2070-2077, January 25, 2008

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Evidence for Annexin II-S100A10 Complex and Plasmin in Mobilization of Cytokine Activity of Human TrpRS^*

Mili Kapoor, Quansheng Zhou, Francella Otero, Christopher A. Myers, Alison Bates, Rajesh Belani, Jianming Liu, Jiann-Kae Luo, Eleni Tzima^¶, Dong-Er Zhang, Xiang-Lei Yang, and Paul Schimmel¹

From the Department of Molecular Biology, The Skaggs Institute for Chemical Biology, and the Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037 and the ^¶Department of Cell and Molecular Physiology, University of North Carolina, Chapel Hill, North Carolina 27599-7545

In mammalian cells, specific aminoacyl-transfer RNA (tRNA) synthetases have cytokine functions that require interactions with partners outside of the translation apparatus. Little is known about these interactions and how they facilitate expanded functions that link protein translation to other cellular pathways. For example, an alternative splice fragment of tryptophanyl-tRNA synthetase (TrpRS) and a similar natural proteolytic fragment are potent angiostatic factors that act through the vascular endothelial-cadherin receptor and Akt signaling pathway. Here we demonstrate mobilization of TrpRS for exocytosis from endothelial cells and the potential for plasmin to activate the cytokine function of the extracellular synthetase. Direct physical evidence showed that the annexin II-S100A10 complex, which regulates exocytosis, forms a ternary complex with TrpRS. Functional studies demonstrate that both annexin II and S100A10 regulate trafficking of TrpRS. Thus, complexes of mammalian tRNA synthetases with seemingly disparate proteins may in general be relevant to understanding how their expanded functions are implemented.

Received for publication, July 23, 2007 , and in revised form, November 6, 2007.

^* This work was supported by Grant CA092577 from the National Cancer Institute of the National Institutes of Health and by a fellowship from the National Foundation for Cancer Research. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables S1 and S2 and supplemental Figs. S1–S4.

¹ To whom correspondence should be addressed: The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-784-8972; Fax: 858-784-8990; E-mail: schimmel{at}scripps.edu.

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