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First published online 28 April 2009
doi: 10.1242/jcs.036103
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Research Article |

1 School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan
2 Department of Bio-science, Nagahama Institute of Bio-science and Technology, Nagahama, Shiga 526-0829, Japan
3 Department of Pharmacology and Neurobiology, Biozentrum, University of Basel, Basel CH-4056, Switzerland
Author for correspondence (e-mail: Tani{at}ls.toyaku.ac.jp)
Accepted 9 February 2009
The presence of subdomains in the endoplasmic reticulum (ER) enables this organelle to perform a variety of functions, yet the mechanisms underlying their organization are poorly understood. In the present study, we show that syntaxin 18, a SNAP (soluble NSF attachment protein) receptor localized in the ER, is important for the organization of two ER subdomains, smooth/rough ER membranes and ER exit sites. Knockdown of syntaxin 18 caused a global change in ER membrane architecture, leading to the segregation of the smooth and rough ER. Furthermore, the organization of ER exit sites was markedly changed concomitantly with dispersion of the ER-Golgi intermediate compartment and the Golgi complex. These morphological changes in the ER were substantially recovered by treatment of syntaxin-18-depleted cells with brefeldin A, a reagent that stimulates retrograde membrane flow to the ER. These results suggest that syntaxin 18 has an important role in ER subdomain organization by mediating the fusion of retrograde membrane carriers with the ER membrane.
Key words: Brefeldin A, COPII, Endoplasmic reticulum, Membrane fusion, Subdomain, Syntaxin 18
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