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Golgi self-correction generates bioequivalent glycans to preserve cellular homeostasis

eLife, ISSN: 2050-084X, Vol: 5, Issue: JUNE2016, Page: e14814
2016
  • 62
    Citations
  • 0
    Usage
  • 70
    Captures
  • 1
    Mentions
  • 63
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    62
  • Captures
    70
  • Mentions
    1
    • News Mentions
      1
      • News
        1
  • Social Media
    63
    • Shares, Likes & Comments
      63
      • Facebook
        63

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Golgi self-correction generates bioequivalent glycans to preserve cellular homeostasis

Research Article ACCEPTED MANUSCRIPT Haik Mkhikian Christie-Lynn Mortales Raymond Zhou Khachik Khachikyan Gang Wu Stuart M Haslam Patil Kavarian Anne Dell Michael Demetriou University of

Article Description

Essential biological systems employ self-correcting mechanisms to maintain cellular homeostasis. Mammalian cell function is dynamically regulated by the interaction of cell surface galectins with branched N-glycans. Here we report that N-glycan branching deficiency triggers the Golgi to generate bioequivalent N-glycans that preserve galectin-glycoprotein interactions and cellular homeostasis. Galectins bind N-acetyllactosamine (LacNAc) units within N-glycans initiated from UDP-GlcNAc by the medial-Golgi branching enzymes as well as the trans-Golgi poly-LacNAc extension enzyme β1,3-N-acetylglucosaminyltransferase (B3GNT). Marginally reducing LacNAc content by limiting N-glycans to three branches results in T-cell hyperactivity and autoimmunity; yet further restricting branching does not produce a more hyperactive state. Rather, new poly-LacNAc extension by B3GNT maintains galectin binding and immune homeostasis. Poly-LacNAc extension is triggered by redistribution of unused UDP-GlcNAc from the medial to trans-Golgi via inter-cisternal tubules. These data demonstrate the functional equivalency of structurally dissimilar N-glycans and suggest a self-correcting feature of the Golgi that sustains cellular homeostasis.

Bibliographic Details

http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84978877847&origin=inward; http://dx.doi.org/10.7554/elife.14814; http://www.ncbi.nlm.nih.gov/pubmed/27269286; https://elifesciences.org/articles/14814#fig6; http://dx.doi.org/10.7554/elife.14814.017; https://elifesciences.org/articles/14814#fig2; http://dx.doi.org/10.7554/elife.14814.005; https://elifesciences.org/articles/14814#abstract; http://dx.doi.org/10.7554/elife.14814.001; https://elifesciences.org/articles/14814#fig4; http://dx.doi.org/10.7554/elife.14814.011; https://elifesciences.org/articles/14814#digest; http://dx.doi.org/10.7554/elife.14814.002; https://elifesciences.org/articles/14814#tbl1; http://dx.doi.org/10.7554/elife.14814.013; https://elifesciences.org/articles/14814#fig7; http://dx.doi.org/10.7554/elife.14814.019; https://elifesciences.org/articles/14814; http://dx.doi.org/10.7554/elife.14814.021; http://dx.doi.org/10.7554/elife.14814.020; https://elifesciences.org/articles/14814#decision-letter; https://cdn.elifesciences.org/articles/14814/elife-14814-v2.pdf; https://cdn.elifesciences.org/articles/14814/elife-14814-v2.xml; https://elifesciences.org/articles/14814#fig5; http://dx.doi.org/10.7554/elife.14814.015; https://elifesciences.org/articles/14814#tbl2; http://dx.doi.org/10.7554/elife.14814.014; https://elifesciences.org/articles/14814#fig3; http://dx.doi.org/10.7554/elife.14814.009; https://elifesciences.org/articles/14814#fig1; http://dx.doi.org/10.7554/elife.14814.003; https://elifesciences.org/articles/14814#author-response; https://dx.doi.org/10.7554/elife.14814

Mkhikian, Haik; Mortales, Christie-Lynn; Zhou, Raymond W; Khachikyan, Khachik; Wu, Gang; Haslam, Stuart M; Kavarian, Patil; Dell, Anne; Demetriou, Michael

eLife Sciences Publications, Ltd

Neuroscience; Biochemistry, Genetics and Molecular Biology; Immunology and Microbiology

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