Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F26%3A00647669" target="_blank" >RIV/61389030:_____/26:00647669 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1093/plcell/koag005" target="_blank" >https://doi.org/10.1093/plcell/koag005</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/plcell/koag005" target="_blank" >10.1093/plcell/koag005</a>
Alternative languages
Result language
angličtina
Original language name
Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth
Original language description
An octameric eukaryotic translation initiation factor 3 subunit E (eIF3E) preserves translational homeostasis through selective messenger RNA (mRNA) recognition and ribosome assembly. Yet, the mechanisms by which eIF3E maintains translational equilibriumremain poorly understood. We show here that eIF3E domain architecture and phosphorylation sites (Thr417, Ser421) are conserved across eukaryotes. Deleting the Proteasome-COP9 signalosome-Initiation factor 3 domain (PCI domain) abolished nuclear localization, disrupted eIF3E–eIF3L interaction, and impaired eIF3E dissociation from the polysomes. Affnity RNA immunoprecipitation sequencing of eIF3E::YFP in tobacco pollen tubes identified mRNAs bearing coding-sequence motifs (MC1 to MC3) that co-immunoprecipitate with eIF3E.Using mRNA reporter assay, we reveal that these motifs act in tandem as eIF3E-dependent translational repressors and enhancers. AlphaFold3 structural modeling and Förster resonance energy transfer verification indicate that PCI domain deletion or PCI-phosphosite mutagenesis weaken eIF3E–eIF3L interactions and block translational activation of MC2 RNA reporter. We further show thatloss of the PCI domain or PCI-phosphosite mutagenesis misregulate pollen tube growth and membrane organization. Together, our findings underscore eIF3E as a selective regulator of mRNA translation that couplescis-motifrecognition to membrane integrityand pollen tube growth, thereby ensuringplant fertility.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10601 - Cell biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2026
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Plant Cell
ISSN
1040-4651
e-ISSN
1532-298X
Volume of the periodical
38
Issue of the periodical within the volume
2
Country of publishing house
US - UNITED STATES
Number of pages
26
Pages from-to
koag005
UT code for WoS article
001691976200001
EID of the result in the Scopus database
2-s2.0-105030415494