Rbm24a dictates mRNA recruitment for germ granule assembly in zebrafish

The germ granules are ribonucleoprotein (RNP) biomolecular condensates that determine the fate of primordial germ cells (PGCs) and serve as a model for studying RNP granule assembly. Here, we show that the maternal RNA-binding protein Rbm24a is a key factor governing the specific sorting of mRNAs into germ granules. Mechanistically, Rbm24a interacts with the germ plasm component Buc to dictate the specific recruitment of germ plasm mRNAs into phase-separated condensates. Germ plasm particles lacking Rbm24a and mRNAs fail to undergo kinesin-dependent transport toward cleavage furrows where small granules fuse into large aggregates. Therefore, the loss of maternal Rbm24a causes a complete degradation of the germ plasm and the disappearance of PGCs. These findings demonstrate that the Rbm24a/Buc complex functions as a nucleating organizer of germ granules, highlighting an emerging mechanism for RNA-binding proteins in reading and recruiting RNA components into a phase-separated protein scaffold.

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Publication Details

Journal
The EMBO Journal
Published
2025-04-25
DOI
https://doi.org/10.1038/s44318-025-00442-z
Citations
4
Primary Topic
RNA Research and Splicing
Type
article
Field-Weighted Citation Impact
3.22

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article

Rbm24a dictates mRNA recruitment for germ granule assembly in zebrafish

Raphaëlle Grifone, Yizhuang Zhang, Dalei Wu, Jiayi Zhou et al.
4 citations
The EMBO Journal
RNA Research and Splicing
3.22
article

Rbm24a dictates mRNA recruitment for germ granule assembly in zebrafish

Raphaëlle Grifone, Yizhuang Zhang, Dalei Wu, Jiayi Zhou, Boya Yang, Panfeng Li, De‐Li Shi, Ming Shao, Ang Li, Shuqi Hu, Chong Zhang, Zhengyang Wang, Tong Lu, Jiasheng Wang, Hailing Fang, Yubin Huang, Qianqian Gong
article en
4 citations

Abstract

The germ granules are ribonucleoprotein (RNP) biomolecular condensates that determine the fate of primordial germ cells (PGCs) and serve as a model for studying RNP granule assembly. Here, we show that the maternal RNA-binding protein Rbm24a is a key factor governing the specific sorting of mRNAs into germ granules. Mechanistically, Rbm24a interacts with the germ plasm component Buc to dictate the specific recruitment of germ plasm mRNAs into phase-separated condensates. Germ plasm particles lacking Rbm24a and mRNAs fail to undergo kinesin-dependent transport toward cleavage furrows where small granules fuse into large aggregates. Therefore, the loss of maternal Rbm24a causes a complete degradation of the germ plasm and the disappearance of PGCs. These findings demonstrate that the Rbm24a/Buc complex functions as a nucleating organizer of germ granules, highlighting an emerging mechanism for RNA-binding proteins in reading and recruiting RNA components into a phase-separated protein scaffold.

The EMBO JournalVol. 44(11)
Qingdao University (CN), Centre National de la Recherche Scientifique (FR), Qingdao Agricultural University (CN), Shandong University (CN), Inserm (FR), Guangdong Medical College (CN), Sorbonne Université (FR), Central People's Hospital of Zhanjiang (CN), Institut de Biologie Paris-Seine (FR), Affiliated Hospital of Qingdao University (CN), Taishan University (CN), Ministry of Education (PT), Institute of Microbial Technology (IN), Qilu Hospital of Shandong University (CN), Développement Adaptation et Vieillissement (FR), Ocean University of China (CN), Shandong University of Science and Technology (CN)
French Muscular Dystrophy Association, National Natural Science Foundation of China, Natural Science Foundation of Shandong Province
Openalex Percentile: Top 9%
RNA Research and Splicing
3.22
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