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J. Biol. Chem., Vol. 278, Issue 23, 20946-20953, June 6, 2003

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The Subunit of the Sec61p Endoplasmic Reticulum Translocon Interacts with the Exocyst Complex in Saccharomyces cerevisiae^*

Jaana H. Toikkanen, Karl Juha Miller, Hans Söderlund, Jussi Jäntti  and Sirkka Keränen 

From the VTT Biotechnology, P. O. Box 1500, FIN-02044 VTT, Finland

The exocyst is a conserved protein complex proposed to mediate vesicle tethering at the plasma membrane. Previously, we identified SEB1/SBH1, encoding the subunit of the Sec61p ER translocation complex, as a multicopy suppressor of the sec15-1 mutant, defective for one subunit of the exocyst complex. Here we show the functional and physical interaction between components of endoplasmic reticulum translocon and the exocytosis machinery. We show that overexpression of SEB1 suppresses the growth defect in all exocyst sec mutants. In addition, overexpression of SEC61 or SSS1 encoding the other two components of the Sec61p complex suppressed the growth defects of several exocyst mutants. Seb1p was coimmunoprecipitated from yeast cell lysates with Sec15p and Sec8p, components of the exocyst complex, and with Sec4p, a secretory vesicle associated Rab GTPase that binds to Sec15p and is essential for exocytosis. The interaction between Seb1p and Sec15p was abolished in sec15-1 mutant and was restored upon SEB1 overexpression. Furthermore, in wild type cells overexpression of SEB1 as well as SEC4 resulted in increased production of secreted proteins. These findings propose a novel functional and physical link between the endoplasmic reticulum translocation complex and the exocyst.

Received for publication, December 23, 2002 , and in revised form, March 24, 2003.

^* This work was supported by the Academy of Finland (Grants 8244, 42160, 49894, and 52096) and the Human Frontier Science Program (RG63/95 to S. K.). This work is part of the research program "VTT Industrial Biotechnology" (Academy of Finland; Finnish Centre of Excellence Program, 2000–2005, Project 64330). 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.

To whom correspondence may also be addressed. Tel.: 358-9-4565225; Fax: 358-9-4552103; E-mail: jussi.jantti{at}vtt.fi.To whom correspondence may be addressed. Tel.: 358-9-4565138; Fax: 358-9-4552103; E-mail:sirkka.keranen{at}vtt.fi.

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