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J. Biol. Chem., Vol. 283, Issue 4, 1857-1861, January 25, 2008

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Molecular Basis of Sugar Recognition by the Human L-type Lectins ERGIC-53, VIPL, and VIP36^*

Yukiko Kamiya¹, Daiki Kamiya, Kazuo Yamamoto^¶, Beat Nyfeler^||2, Hans-Peter Hauri^||3, and Koichi Kato^**4

From the Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan, CREST, Japan Science and Technology Corporation, 4-1-8 Honcho, Kawaguchi 332-1102, Japan, the ^¶Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan, ^||Biozentrum, University of Basel, CH-4056 Basel, Switzerland, the ^**Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi 444-8787, Japan, the Glycoscience Institute, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan, and GLYENCE Company, Limited, 2-22-8, Chikusa, Chikusa-ku, Nagoya 474-0858, Japan

ERGIC-53, VIPL, and VIP36 are related type 1 membrane proteins of the mammalian early secretory pathway. They are classified as L-type lectins because of their luminal carbohydrate recognition domain, which exhibits homology to leguminous lectins. These L-type lectins have different intracellular distributions and dynamics in the endoplasmic reticulum-Golgi system of the secretory pathway and interact with N-glycans of glycoproteins in a Ca²⁺-dependent manner, suggesting a role in glycoprotein sorting and trafficking. To understand the function of these lectins, knowledge of their carbohydrate specificity is crucial but only available for VIP36 (Kamiya, Y., Yamaguchi, Y., Takahashi, N., Arata, Y., Kasai, K. I., Ihara, Y., Matsuo, I., Ito, Y., Yamamoto, K., and Kato, K. (2005) J. Biol. Chem. 280, 37178–37182). Here we provide a comprehensive and quantitative analysis of sugar recognition of the carbohydrate recognition domains of ERGIC-53 and VIPL in comparison with VIP36 using a pyridylaminated sugar library in conjunction with frontal affinity chromatography. Frontal affinity chromatography revealed selective interaction of VIPL and VIP36 with the deglucosylated trimannose in the D1 branch of high-mannose-type oligosaccharides but with different pH dependence. ERGIC-53 bound high-mannose-type oligosaccharides with low affinity and broad specificity, not discriminating between monoglucosylated and deglucosylated high-mannosetype oligosaccharides. Based on the sugar-binding properties in conjunction with known features of these proteins, we propose a model for the action of the three lectins in glycoprotein guidance and trafficking. Moreover, structure-based mutagenesis revealed that the sugar-binding properties of these L-type lectins can be switched by single amino acid substitutions.

Received for publication, November 15, 2007

^* This work was supported in part by Grants-in-aid for Scientific Research 15032249, 17046017, and 18390016 from the Ministry of Education, Culture, Sports, Science, and Technology of Japan and by a grant-in-aid for research from Nagoya City University. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2 and additional references.

¹ Recipient of Japan Society for the Promotion of Science Research Fellow-ships for Young Scientists.

² Supported by a Roche Research Foundation fellowship.

³ Supported by the Swiss National Science Foundation and the University of Basel.

⁴ To whom correspondence should be addressed: Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan. Tel./Fax: 81-52-836-3447; E-mail: kkato{at}phar.nagoya-cu.ac.jp.

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