IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-62768-w.html
   My bibliography  Save this article

Enzymatic craftsmanship in collagen glycosylation

Author

Listed:
  • Susovon Ghosh

    (Indian Institute of Technology (IIT) Mandi)

  • Dilip Kumar

    (Ashoka University)

  • Bhaskar Mondal

    (Indian Institute of Technology (IIT) Mandi)

  • Trayambak Basak

    (Indian Institute of Technology (IIT) Mandi)

Abstract

Collagen IV, a key structural protein of basement membranes, is vital for the development and survival of multicellular life forms. Its maturation relies on specific post-translational O- glycosylation, primarily mediated by lysyl hydroxylase-3 (LH3) and other glycosyltransferases, which sculpt collagen by modifying the hydroxylysine residues with sugar moieties.

Suggested Citation

  • Susovon Ghosh & Dilip Kumar & Bhaskar Mondal & Trayambak Basak, 2025. "Enzymatic craftsmanship in collagen glycosylation," Nature Communications, Nature, vol. 16(1), pages 1-4, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-62768-w
    DOI: 10.1038/s41467-025-62768-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-62768-w
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-025-62768-w?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Hou-Fu Guo & Chi-Lin Tsai & Masahiko Terajima & Xiaochao Tan & Priyam Banerjee & Mitchell D. Miller & Xin Liu & Jiang Yu & Jovita Byemerwa & Sarah Alvarado & Tamer S. Kaoud & Kevin N. Dalby & Neus Bot, 2018. "Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    2. Matteo De Marco & Sristi Raj Rai & Luigi Scietti & Daiana Mattoteia & Stefano Liberi & Elisabetta Moroni & Alberta Pinnola & Alice Vetrano & Claudio Iacobucci & Carlo Santambrogio & Giorgio Colombo & , 2025. "Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1," Nature Communications, Nature, vol. 16(1), pages 1-17, December.
    3. Luigi Scietti & Antonella Chiapparino & Francesca De Giorgi & Marco Fumagalli & Lela Khoriauli & Solomon Nergadze & Shibom Basu & Vincent Olieric & Lucia Cucca & Blerida Banushi & Antonella Profumo & , 2018. "Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    4. Luigi Scietti & Antonella Chiapparino & Francesca Giorgi & Marco Fumagalli & Lela Khoriauli & Solomon Nergadze & Shibom Basu & Vincent Olieric & Lucia Cucca & Blerida Banushi & Antonella Profumo & Ele, 2018. "Author Correction: Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3," Nature Communications, Nature, vol. 9(1), pages 1-1, December.
    5. Junjiang Peng & Wenguo Li & Deqiang Yao & Ying Xia & Qian Wang & Yan Cai & Shaobai Li & Mi Cao & Yafeng Shen & Peixiang Ma & Rijing Liao & Jie Zhao & An Qin & Yu Cao, 2025. "The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Jeong Seon Kim & Zhenhang Chen & Sara Andrea Espinosa Garcia & Christoph Buhlheller & Botao Zhang & Stephen J. Richards & Tingfei Chen & Jingjing Wu & Ronald C. Bruntz & Marisa E. Gilliam & Mitsuo Yam, 2025. "Structural basis of collagen glucosyltransferase function and its serendipitous role in kojibiose synthesis," Nature Communications, Nature, vol. 16(1), pages 1-11, December.
    2. Matteo De Marco & Sristi Raj Rai & Luigi Scietti & Daiana Mattoteia & Stefano Liberi & Elisabetta Moroni & Alberta Pinnola & Alice Vetrano & Claudio Iacobucci & Carlo Santambrogio & Giorgio Colombo & , 2025. "Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1," Nature Communications, Nature, vol. 16(1), pages 1-17, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-62768-w. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.