Ontology highlight
ABSTRACT:
PROVIDER: PRJNA540320 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR13873630_1.fastq.gz | Fastqsanger.gz | |||
| SRR13873630_2.fastq.gz | Fastqsanger.gz | |||
| SRR13873631_1.fastq.gz | Fastqsanger.gz | |||
| SRR13873631_2.fastq.gz | Fastqsanger.gz | |||
| SRR13873632.fastq.gz | Fastqsanger.gz |
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Project description:SAYSD1 senses UFMylated ribosome to safeguard co-translational protein translocation at the endoplasmic reticulum
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Project description:Co-translational targeting by the signal recognition particle delivers nascent secretory and membrane proteins into the endoplasmic reticulum, yet its role in mammalian germ cells remains unclear. Here, we found that SRP68 is indispensable for spermatogenesis in mice. Conditional Srp68 deletion in germ cells results in defective synapsis and double-strand break repair, leading to meiotic prophase I arrest and male infertility. Proteomic profiling revealed that SRP68-deficient spermatocytes exhibit significant reduced endoplasmic reticulum (ER)-associated signal peptide-containing proteins, accompanied by structural disorganization. Additionally, multiple factors involved in ER–mitochondrial contact are decreased in SRP68-deficient spermatocytes, leading to mitochondrial calcium ion depletion, depolarized membrane potential, and insufficient ATP production. These findings demonstrate that SRP68-dependent co-translational targeting is essential for meiotic progression, providing a basis for interpreting ER-related causes of male infertility.
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Project description:IRE1, alongside ATF6 and PERK, orchestrates the unfolded protein response, a network of signaling pathways that maintains endoplasmic reticulum (ER) homeostasis. Two modes of IRE1 activation are known: i) in response to an accumulation of unfolded proteins in the ER lumen and ii) in response to compositional changes to the ER membrane that alter its physical properties. Here, we identify a third, independent mode of IRE1 activation: ER co-translational translocation deficits activate IRE1 through a mechanism that relies on the release of IRE1 molecules from unoccupied translocons. We define this mechanism as TRES for “TRanslocon Engagement Surveillance”. TRES leads to spontaneous activation of IRE1 and bypasses its unfolded protein- and ER membrane composition-sensing functions. Inhibiting translation initiation similarly activates IRE1 by TRES, as it leads to a decline in ER protein import, thus linking the integrated stress response (ISR) to IRE1 signaling. Surprisingly, TRES drives IRE1 activation without activating ATF6 or PERK, resulting in a distinct gene expression program that feeds back into the co-translational translocation pathway to rebalance the ER protein load. Our findings demonstrate that monitoring and adjusting the rates of protein translocation are critical for maintaining ER homeostasis.
2026-03-09 | GSE323963 | GEO
Project description:IRE1, alongside ATF6 and PERK, orchestrates the unfolded protein response, a network of signaling pathways that maintains endoplasmic reticulum (ER) homeostasis. Two modes of IRE1 activation are known: i) in response to an accumulation of unfolded proteins in the ER lumen and ii) in response to compositional changes to the ER membrane that alter its physical properties. Here, we identify a third, independent mode of IRE1 activation: ER co-translational translocation deficits activate IRE1 through a mechanism that relies on the release of IRE1 molecules from unoccupied translocons. We define this mechanism as TRES for “TRanslocon Engagement Surveillance”. TRES leads to spontaneous activation of IRE1 and bypasses its unfolded protein- and ER membrane composition-sensing functions. Inhibiting translation initiation similarly activates IRE1 by TRES, as it leads to a decline in ER protein import, thus linking the integrated stress response (ISR) to IRE1 signaling. Surprisingly, TRES drives IRE1 activation without activating ATF6 or PERK, resulting in a distinct gene expression program that feeds back into the co-translational translocation pathway to rebalance the ER protein load. Our findings demonstrate that monitoring and adjusting the rates of protein translocation are critical for maintaining ER homeostasis.
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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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Project description:Localized protein synthesis is a fundamental mechanism for creating distinct subcellular environments. Here we developed a generalizable proximity-specific ribosome profiling strategy that enables global interrogation of translation in defined subcellular locations. We applied this approach to the endoplasmic reticulum (ER) in yeast and mammals. We observed the vast majority of secretory proteins to be co-translationally translocated, including substrates capable of post-translational insertion in vitro. Distinct translocon complexes engaged nascent chains at different points during synthesis. Whereas most proteins engaged the ER immediately following or even before signal sequence (SS) emergence, a class of Sec66-dependent proteins entered with a looped SS conformation. Finally, we observed rapid ribosome exchange into the cytosol following translation termination. These data provide insights into how distinct translocation mechanisms act in concert to promote efficient co-translational recruitment.
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