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RNF126 Promotes Endoplasmic Reticulum Stress in Fetal Growth Restriction via Ubiquitination-Mediated Degradation of the MYH9/MYH10 Complex

ABSTRACT: RNF126 Promotes Endoplasmic Reticulum Stress in Fetal Growth Restriction via Ubiquitination-Mediated Degradation of the MYH9/MYH10 Complex

PROVIDER: PRJNA1206163 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31884979_1.fastq.gz	Fastqsanger.gz
	SRR31884979_2.fastq.gz	Fastqsanger.gz
	SRR31884980_1.fastq.gz	Fastqsanger.gz
	SRR31884980_2.fastq.gz	Fastqsanger.gz
	SRR31884981_1.fastq.gz	Fastqsanger.gz

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RNF126 Promotes Endoplasmic Reticulum Stress in Fetal Growth Restriction via Ubiquitination-Mediated Degradation of the MYH9/MYH10 Complex

Project description:Fetal growth restriction (FGR) stands as a prominent cause of neonatal morbidity and mortality, yet its underlying mechanisms remain elusive. Through a multi-omics analysis of the human placentas, including quantitative proteomics and ubiquitination-modified proteomics, our team find that the E3 ligase Ring finger protein 126 (RNF126) might be a potentially pivotal protein in the development of FGR. Here, we have discovered that RNF126 can induce endoplasmic reticulum stress (ERS) in placental trophoblasts through RNA sequencing, leading to an increase in apoptosis rates. Subsequent studies have confirmed that RNF126 promotes the degradation of the MYH9/MYH10 complex via the ubiquitin-proteasome pathway, thereby contributing to ERS and inducing trophoblast dysfunction. Meanwhile, Our RNF126 placenta-specific knockout mouse model (cKO) validates these findings in vivo. These events significantly contribute to the occurrence and progression of FGR. This study provides new insights and highlights the promising potential of RNF126 as a therapeutic target for FGR treatment.

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The SND proteins constitute an alternative targeting route to the endoplasmic reticulum

Project description:In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae, and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible.

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