SMG7 and eIF4A constitute a homeostatic module controlling P-body condensation and function of meiotic bodies
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F26%3A00144779" target="_blank" >RIV/00216224:14740/26:00144779 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41467-026-72218-w" target="_blank" >https://www.nature.com/articles/s41467-026-72218-w</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-026-72218-w" target="_blank" >10.1038/s41467-026-72218-w</a>
Alternative languages
Result language
angličtina
Original language name
SMG7 and eIF4A constitute a homeostatic module controlling P-body condensation and function of meiotic bodies
Original language description
Processing bodies (P-bodies) are ribonucleoprotein condensates that regulate RNA processing and storage. Although constitutively present in most cells, their size and composition change dynamically in response to developmental and environmental cues. However, mechanisms governing P-body assembly and remodeling remain poorly understood. Here we show that in Arabidopsis, SMG7 interacts with the eIF4A helicases and recruits them to P-bodies. eIF4As limit P-body condensation and also restrict stress granule (SG) formation under heat stress. We further identify meiotic bodies (M-bodies) as composite RNP granules with a P-body core surrounded by a SG-like shell. The SMG7-eIF4A module regulates the recruitment of the meiosis-specific protein TDM1 into M-bodies, thereby influencing meiotic exit and plant reproduction. Our findings suggest that SMG7 functions as an adaptor protein that recruits client proteins into P-bodies and, together with eIF4A, forms a regulatory module that controls P-body composition and maintains their size homeostasis.
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
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
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
Nature Communications
ISSN
2041-1723
e-ISSN
2041-1723
Volume of the periodical
17
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
19
Pages from-to
1-19
UT code for WoS article
001798426500011
EID of the result in the Scopus database
2-s2.0-105042395980