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MBC in Press, published online ahead of print September 6, 2006
Mol. Biol. Cell 10.1091/mbc.E06-05-0444

A more recent version of this article appeared on November 1, 2006
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Submitted on May 22, 2006
Revised on August 8, 2006
Accepted on August 29, 2006

The Ca2+-binding Protein ALG-2 Is Recruited to ER Exit Sites by Sec31A and Stabilizes the Localization of Sec31A

Akinori Yamasaki,* Katsuko Tani,{dagger} Akitsugu Yamamoto,{ddagger} Naomi Kitamura,* and Masayuki Komada*

*Department of Biological Sciences, Tokyo Institute of Technology, Yokohama 226-8501, Japan; {dagger}School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji 192-0392, Japan; {ddagger}Department of Bio-science, Nagahama Institute of Bio-science and Technology, Nagahama 526-0829, Japan

Monitoring Editor: Randy Schekman

The formation of transport vesicles that bud from endoplasmic reticulum (ER) exit sites is dependent on the COPII coat comprising three components: the small GTPase Sar1, the Sec23/24 complex, and the Sec13/31 complex. Here we provide evidence that ALG-2, a Ca2+-binding protein of unknown function, regulates the COPII function at ER exit sites in mammalian cells. ALG-2 bound to the Prorich region of Sec31A, a ubiquitously expressed mammalian ortholog of yeast Sec31, in a Ca2+-dependent manner and colocalized with Sec31A at ER exit sites. A Ca2+ binding-deficient ALG-2 mutant, which did not bind Sec31A, lost the ability to localize to ER exit sites. Overexpression of the Prorich region of Sec31A or RNA interference-mediated Sec31A depletion also abolished the ALG-2 localization at these sites. On the other hand, depletion of ALG-2 substantially reduced the level of Sec31A associated with the membrane at ER exit sites. Finally, treatment with a cell-permeable Ca2+ chelator caused the mislocalization of ALG-2, which was accompanied by a reduced level of Sec31A at ER exit sites. We conclude that ALG-2 is recruited to ER exit sites via Ca2+-dependent interaction with Sec31A and in turn stabilizes the localization of Sec31A at these sites.

Address correspondence to: Masayuki Komada (makomada{at}bio.titech.ac.jp)




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