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N-glycans Regulate Integrin α5β1 Functions

  • Jianguo Gu
  • Yuya Sato
  • Tomoya Isaji

Abstract

Integrin, which is formed by α and β subunits, is cell surface transmembrane glycoprotein that functions as an adhesion receptor. Integrin engagement during cell adhesion leads to intracellular phosphorylation, such as the phosphorylation of the focal adhesion kinase, thereby regulating gene expression, cell growth, differentiation and survival. Integrin is a major carrier of N-glycans. A growing body of evidence indicates that the N-glycosylation of integrin α5β1 plays crucial roles in hetero-dimer formation and in its biological functions (Gu and Taniguchi 2004). In fact, α5β1 integrin contains 26 potential N-linked glycosylation sites, 14 in the α5 subunit and 12 in the β1 subunit. To determine which of the N-glycosylation sites on the α5 subunit are essential for these functions, we sequentially mutated one or combined asparagines (N) residues in the putative N-glycosylation sites to glutamine (Q) residues as shown in Fig. 1, then transfected these mutant genes into α5-deficient Chinese hamster ovary (CHO) cells (CHO-B2) for cell spreading assay (Isaji et al. 2006).

Keywords

Focal Adhesion Kinase Chinese Hamster Ovary Intracellular Phosphorylation Propeller Domain Core Fucosylation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. Gu J, Taniguchi N (2004) Regulation of integrin functions by N-glycans. Glycoconj J 21:9–15PubMedCrossRefGoogle Scholar
  2. Isaji T, Sato Y, Zhao Y, Miyoshi E, Wada Y, Taniguchi N, Gu J (2006) N-glycosylation of the beta-propeller domain of the integrin alpha5 subunit is essential for alpha5beta1 heterodimerization, expression on the cell surface, and its biological function. J Biol Chem 281:33258–33267PubMedCrossRefGoogle Scholar
  3. Zhao Y, Itoh S, Wang X, Isaji T, Miyoshi E, Kariya Y, Miyazaki K, Kawasaki N, Taniguchi N, Gu J (2006a) Deletion of core fucosylation on alpha3beta1 integrin down-regulates its functions. J Biol Chem 281:38343–38350PubMedCrossRefGoogle Scholar
  4. Zhao Y, Nakagawa T, Itoh S, Inamori K, Isaji T, Kariya Y, Kondo A, Miyoshi E, Miyazaki K, Kawasaki N et al (2006b) N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration. J Biol Chem 281:32122–32130PubMedCrossRefGoogle Scholar

Copyright information

© Springer 2008

Authors and Affiliations

  • Jianguo Gu
    • 1
  • Yuya Sato
    • 1
  • Tomoya Isaji
    • 1
  1. 1.Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and GlycobiologyTohoku Pharmaceutical UniversitySendai, MiyagiJapan

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