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The retromer and retriever systems are conserved and differentially expanded in parabasalids

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F24%3A00588221" target="_blank" >RIV/60077344:_____/24:00588221 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/24:10482855

  • Result on the web

    <a href="https://doi.org/10.1242/jcs.261949" target="_blank" >https://doi.org/10.1242/jcs.261949</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1242/jcs.261949" target="_blank" >10.1242/jcs.261949</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The retromer and retriever systems are conserved and differentially expanded in parabasalids

  • Original language description

    Early endosomes sort transmembrane cargo either for lysosomal degradation or retrieval to the plasma membrane or the Golgi complex. Endosomal retrieval in eukaryotes is governed by the anciently homologous retromer or retriever complexes. Each comprises a core tri-protein subcomplex, membrane-deformation proteins and interacting partner complexes, together retrieving a variety of known cargo proteins. Trichomonas vaginalis, a sexually transmitted human parasite, uses the endomembrane system for pathogenesis. It has massively and selectively expanded its endomembrane protein complement, the evolutionary path of which has been largely unexplored. Our molecular evolutionary study of retromer, retriever and associated machinery in parabasalids and its free-living sister lineage of Anaeramoeba demonstrates specific expansion of the retromer machinery, contrasting with the retriever components. We also observed partial loss of the Commander complex and sorting nexins in Parabasalia but complete retention in Anaeramoeba. Notably, we identified putative parabasalid sorting nexin analogs. Finally, we report the first retriever protein localization in a non-metazoan group along with retromer protein localization in T. vaginalis.

  • 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

    10606 - Microbiology

Result continuities

  • Project

    <a href="/en/project/EF16_019%2F0000759" target="_blank" >EF16_019/0000759: Centre for research of pathogenicity and virulence of parasites</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

    Journal of Cell Science

  • ISSN

    0021-9533

  • e-ISSN

    1477-9137

  • Volume of the periodical

    137

  • Issue of the periodical within the volume

    13

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    15

  • Pages from-to

    jcs261949

  • UT code for WoS article

    001274398200008

  • EID of the result in the Scopus database

    2-s2.0-85198756252