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A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F24%3A10483328" target="_blank" >RIV/00216208:11110/24:10483328 - isvavai.cz</a>

  • Alternative codes found

    RIV/00064165:_____/24:10483328

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=J1ZHjO198v" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=J1ZHjO198v</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.cell.2024.04.041" target="_blank" >10.1016/j.cell.2024.04.041</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis

  • Original language description

    Dolichol is a lipid critical for N-glycosylation as a carrier for activated sugars and nascent oligosaccharides. It is commonly thought to be directly produced from polyprenol by the enzyme SRD5A3. Instead, we found that dolichol synthesis requires a three-step detour involving additional metabolites, where SRD5A3 catalyzes only the second reaction. The first and third steps are performed by DHRSX, whose gene resides on the pseudoautosomal regions of the X and Y chromosomes. Accordingly, we report a pseudoautosomal-recessive disease presenting as a congenital disorder of glycosylation in patients with missense variants in DHRSX (DHRSX-CDG). Of note, DHRSX has a unique dual substrate and cofactor specificity, allowing it to act as a NAD +-dependent dehydrogenase and as a NADPH-dependent reductase in two non-consecutive steps. Thus, our work reveals unexpected complexity in the terminal steps of dolichol biosynthesis. Furthermore, we provide insights into the mechanism by which dolichol metabolism defects contribute to disease.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30100 - Basic medicine

Result continuities

  • Project

    <a href="/en/project/NU22-07-00474" target="_blank" >NU22-07-00474: Molecular genetic causes and biochemical consequences of Congenital disorders of glycosylation</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2024

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Cell

  • ISSN

    0092-8674

  • e-ISSN

    1097-4172

  • Volume of the periodical

    187

  • Issue of the periodical within the volume

    14

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    40

  • Pages from-to

    3585-"3601.e22"

  • UT code for WoS article

    001272252900001

  • EID of the result in the Scopus database

    2-s2.0-85195665598