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Published online
doi:10.1083/jcb.200704078
The Journal of Cell Biology, Vol. 180, No. 1, 129-143
The Rockefeller University Press, 0021-9525 $30.00
© Nagaya et al.
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Article

Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum



Hisao Nagaya1,3, Taku Tamura1,3, Arisa Higa-Nishiyama1,3, Koji Ohashi1,3, Mayumi Takeuchi1,3, Hitoshi Hashimoto1,3, Kiyotaka Hatsuzawa1,3, Masataka Kinjo4, Tatsuya Okada2, and Ikuo Wada1,3

1 Department of Cell Science, Institute of Biomedical Sciences, and 2 Department of Mathematics, Fukushima Medical University School of Medicine, Fukushima 960-1295, Japan
3 Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan
4 Research Institute for Electronic Science, Hokkaido University, Sapporo 060-0812, Japan

Correspondence to Ikuo Wada: iwada{at}fmu.ac.jp

The quality of cargo proteins in the endoplasmic reticulum (ER) is affected by their motion during folding. To understand how the diffusion of secretory cargo proteins is regulated in the ER, we directly analyze the motion of a single cargo molecule using fluorescence imaging/fluctuation analyses. We find that the addition of two N-glycans onto the cargo dramatically alters their diffusion by transient binding to membrane components that are confined by hyperosmolarity. Via simultaneous observation of a single cargo and ER exit sites (ERESs), we could exclude ERESs as the binding sites. Remarkably, actin cytoskeleton was required for the transient binding. These results provide a molecular basis for hypertonicity-induced immobilization of cargo, which is dependent on glycosylation at multiple sites but not the completion of proper folding. We propose that diffusion of secretory glycoproteins in the ER lumen is controlled from the cytoplasm to reduce the chances of aggregation.

Abbreviations used in this paper: ERES, ER exit site; EYFP, enhanced YFP; FCS, fluorescence correlation spectroscopy; FLIP, fluorescence loss induced by photobleaching; LAT, latrunculin B; MSD, mean square displacement; TIRFM, total internal reflection fluorescence microscopy; VSVG, vesicular stomatitis virus glycoprotein; YE, EYFP-ER.


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