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Glycobiology Advance Access originally published online on June 22, 2007
Glycobiology 2007 17(9):913-921; doi:10.1093/glycob/cwm067
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Stable interaction of the cargo receptor VIP36 with molecular chaperone BiP

Daisuke Nawa2, Osamu Shimada3, Norihito Kawasaki2, Naoki Matsumoto2 and Kazuo Yamamoto1,2,4,

2 Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba 277-8562, Japan
3 Department of Anatomy, Yamanashi University School of Medicine, Tamaho-cho 1110, Yamanashi 409-3898, Japan
4 CREST, JST, Honcho 4-1-8, Kawaguchi 332-1102, Japan

1 To whom correspondence should be addressed: Tel: +81-4-7136-3614 Fax: +81-4-7136-3619; e-mail: yamamoto{at}k.u-tokyo.ac.jp

Received on February 26, 2007; revised on June 16, 2007; accepted on June 17, 2007

VIP36 is an intracellular lectin that cycles between the endoplasmic reticulum (ER) and the Golgi apparatus, and is thought to act as a cargo receptor in the transport and sorting of glycoproteins. Here we sought to identify the proteins that interact with VIP36 during the quality control of secretory proteins. VIP36 was crosslinked and immunoprecipitated from HEK293 cells that expressed Myc-tagged VIP36. An ~80 kDa protein coprecipitated with VIP36 and LC/MS/MS analysis revealed it to be immunoglobulin-binding protein (BiP), a major protein of the Hsp70 chaperone family. A VIP36 mutant with defective lectin activity was also proficient for the coimmunoprecipitation of an equivalent amount of BiP, indicating that the interaction between VIP36 and BiP was carbohydrate-independent. Immunoelectron microscopy experiment demonstrated that the interaction between VIP36 and BiP occurred in the ER. However, the VIP36 coprecipitated with BiP was resistant to endo ß-N-acetylglucosaminidase H treatment. A pulse-chase experiment revealed that the amount of BiP interacting with VIP36 did not change over more than 2 h. These results suggest that the interaction of VIP36 and BiP is not due to chaperone–substrate complex. Surface plasmon resonance analysis using recombinant proteins confirmed these binding characteristics of VIP36 and BiP in vitro. The interaction between recombinant soluble VIP36 and BiP is dependent on divalent cations but not on ATP. This mode of interaction is also different from that observed between BiP and its chaperone substrates. These observations suggest a new role for VIP36 in the quality control of secretory proteins.

Key words: BiP / cargo receptor / chaperone / interaction / VIP36


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