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Vol. 11, Issue 3, 983-998, March 2000

Sec24p and Iss1p Function Interchangeably in Transport Vesicle Formation from the Endoplasmic Reticulum in Saccharomyces cerevisiae

Tatsuo Kurihara,^* Susan Hamamoto,^* Ruth E. Gimeno,^§ Chris A. Kaiser, Randy Schekman,^* and Tohru Yoshihisa^*¶

 ^*Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, California 94720; and  Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

The Sec23p/Sec24p complex functions as a component of the COPII coat in vesicle transport from the endoplasmic reticulum. Here we characterize Saccharomyces cerevisiae SEC24, which encodes a protein of 926 amino acids (YIL109C), and a close homologue, ISS1 (YNL049C), which is 55% identical to SEC24. SEC24 is essential for vesicular transport in vivo because depletion of Sec24p is lethal, causing exaggeration of the endoplasmic reticulum and a block in the maturation of carboxypeptidase Y. Overproduction of Sec24p suppressed the temperature sensitivity of sec23-2, and overproduction of both Sec24p and Sec23p suppressed the temperature sensitivity of sec16-2. SEC24 gene disruption could be complemented by overexpression of ISS1, indicating functional redundancy between the two homologous proteins. Deletion of ISS1 had no significant effect on growth or secretion; however, iss1 mutants were found to be synthetically lethal with mutations in the v-SNARE genes SEC22 and BET1. Moreover, overexpression of ISS1 could suppress mutations in SEC22. These genetic interactions suggest that Iss1p may be specialized for the packaging or the function of COPII v-SNAREs. Iss1p tagged with His₆ at its C terminus copurified with Sec23p. Pure Sec23p/Iss1p could replace Sec23p/Sec24p in the packaging of a soluble cargo molecule (-factor) and v-SNAREs (Sec22p and Bet1p) into COPII vesicles. Abundant proteins in the purified vesicles produced with Sec23p/Iss1p were indistinguishable from those in the regular COPII vesicles produced with Sec23p/Sec24p.

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Corresponding author. E-mail address: schekman{at}uclink4.berkeley.edu.

Present addresses: Institute for Chemical Research, Kyoto University, Kyoto, Japan;

^§ Millennium Pharmaceuticals, Inc., Cambridge, MA 02139;

^¶ Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya, Japan.

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Molecular Biology of the Cell
Vol. 11, 983-998, March 2000
Copyright © 2000 by The American Society for Cell Biology

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