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MBC in Press, published online ahead of print December 27, 2006
Mol. Biol. Cell 10.1091/mbc.E06-08-0707

A more recent version of this article appeared on March 1, 2007
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Submitted on August 15, 2006
Revised on November 22, 2006
Accepted on December 18, 2006

Two Mammalian Sec16 Homologs Have Nonredundant Functions in ER Export and Transitional ER Organization

Dibyendu Bhattacharyya and Benjamin S. Glick

Department of Molecular Genetics and Cell Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637

Monitoring Editor: Francis Barr

Budding yeast Sec16 is a large peripheral ER membrane protein that functions in generating COPII transport vesicles and in clustering COPII components at transitional ER (tER) sites. Sec16 interacts with multiple COPII components. Although the COPII assembly pathway is evolutionarily conserved, Sec16 homologues have not been described in higher eukaryotes. Here we show that mammalian cells contain two distinct Sec16 homologues: a large protein that we term Sec16L and a smaller protein that we term Sec16S. These proteins localize to tER sites, and an N-terminal region of each protein is necessary and sufficient for tER localization. The Sec16L and Sec16S genes are both expressed in every tissue examined, and both proteins are required in HeLa cells for ER export and for normal tER organization. Sec16L resembles yeast Sec16 in having a C-terminal conserved domain that interacts with the COPII coat protein Sec23, but Sec16S lacks such a C-terminal conserved domain. Immunoprecipitation data indicate that Sec16L and Sec16S are each present at multiple copies in a heteromeric complex. We infer that mammalian cells have preserved and extended the conserved function of Sec16.

Address correspondence to: Benjamin S. Glick (bsglick{at}uchicago.edu)




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