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J. Biol. Chem., Vol. 281, Issue 44, 33621-33634, November 3, 2006

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Kinectin-dependent Assembly of Translation Elongation Factor-1 Complex on Endoplasmic Reticulum Regulates Protein Synthesis^*

Lee-Lee Ong¹, Pao-Chun Lin^¶, Xin Zhang^||1, Ser-Mien Chia, and Hanry Yu^||¶**2

From the National University Medical Institutes, Department of Physiology, ^||Graduate Program in Bioengineering, ^¶NUS Graduate School of Integrative Sciences and Engineering, and ^**NUSTEP, National University of Singapore Singapore 117597, Singapore, the Singapore-MIT Alliance, Singapore 117576, Singapore, and the Institute of Bioengineering and Nanotechnology, Agency for Science, Technology, and Research, Singapore 138669, Singapore

Kinectin is an integral membrane protein with many isoforms primarily found on the endoplasmic reticulum. It has been found to bind kinesin, Rho GTPase, and translation elongation factor-1. None of the existing models for the quaternary organization of the elongation factor-1 complex in higher eukaryotes involves kinectin. We have investigated here the assembly of the elongation factor-1 complex onto endoplasmic reticulum via kinectin using in vitro and in vivo assays. We established that the entire elongation factor-1 complex can be anchored to endoplasmic reticulum via kinectin, and the interacting partners are as follows. Kinectin binds EF-1, which in turn binds EF-1 but not EF-1; EF-1 binds EF-1 and EF-1 but not kinectin. In vivo splice blocking of the kinectin exons 36 and 37 produced kinectin lacking the EF-1 binding domain, which disrupted the membrane localization of EF-1, EF-1, and EF-1 on endoplasmic reticulum, similar to the disruptions seen with the overexpression of kinectin fragments containing the EF-1 binding domain. The disruptions of the EF-1/kinectin interaction inhibited expression of membrane proteins but enhanced synthesis of cytosolic proteins in vivo. These findings suggest that anchoring the elongation factor-1 complex onto endoplasmic reticulum via EF-1/kinectin interaction is important for regulating protein synthesis in eukaryotic cells.

Received for publication, August 8, 2006

^* This work was supported in part by National Medical Research Council of Singapore Grant R185-000-099-213, Academic Research Council, Ministry of Education of Singapore Grant R185-000-135-112, Biomedical Medical Research Council of Singapore Grant R185-000-045-305, and intramural funding through the Institute of Bioengineering and Nanotechnology (to H. Y. U.). 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 Figs. 1 and 2.

¹ Graduate Research Scholar of the National University of Singapore.

² To whom correspondence should be addressed: Dept. of Physiology, National University of Singapore, Block MD11, 04-01A, 10 Medical Dr., Singapore 117597. Tel.: 65-6516-3466; Fax: 65-6872-7150; E-mail: phsyuh{at}nus.edu.sg.

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