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A more recent version of this article appeared on November 4, 2005
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M505757200v1
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Papers In Press, published online ahead of print August 29, 2005
J. Biol. Chem, 10.1074/jbc.M505757200
Submitted on May 26, 2005
Accepted on August 29, 2005

Sugar-binding properties of VIP36, an intracellular animal lectin operating as a cargo receptor

Yukiko Kamiya, Yoshiki Yamaguchi, Noriko Takahashi, Yoichiro Arata, Ken-ichi Kasai, Yoshito Ihara, Ichiro Matsuo, Yukishige Ito, Kuzuo Yamamoto, and Koichi Kato

Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi 467-0863

Corresponding Author: kkato{at}phar.nagoya-cu.ac.jp

The vesicular integral protein of 36 kDa (VIP36) is an intracellular animal lectin, which acts as a putative cargo receptor recycling between the Golgi and the endoplasmic reticulum (ER). Although VIP36 interacts with glycoproteins carrying high mannose type oligosaccharides, detailed analyses of sugar-binding specificity discriminating isomeric oligosaccharide structures have not been performed yet. In the present study, we have analyzed sugar-binding properties of a recombinant carbohydrate recognition domain of VIP36 (VIP36-CRD) by frontal affinity chromatography (FAC) method. For this purpose, a pyridylaminated sugar library, consisting 21 kinds of oligosaccharides including isomeric structures, was prepared and subjected to FAC analyses. The FAC data has shown that glucosylation and trimming of the D1 mannosyl branch interfere with the binding of VIP36-CRD. VIP36-CRD exhibits a bell-shaped pH dependence of sugar-binding with optimal pH around 6.5. By inspection of the specificity and optimal pH of sugar-binding of VIP36 and its subcellular localization, together with the organeller pH, we suggest that VIP36 binds glycoproteins retaining the intact D1 mannosyl branch in the cis-Golgi network and recycles to the ER, where it releases the cargos due to higher pH, thereby contributing to quality control of glycoproteins.


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