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A phosphorylation-regulated eIF3d translation switch mediates cellular adaptation to metabolic stress

ABSTRACT: A phosphorylation-regulated eIF3d translation switch mediates cellular adaptation to metabolic stress

PROVIDER: PRJNA664584 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12678312.fastq.gz	Fastqsanger.gz
	SRR12678313.fastq.gz	Fastqsanger.gz
	SRR12678314.fastq.gz	Fastqsanger.gz
	SRR12678315.fastq.gz	Fastqsanger.gz
	SRR12678316.fastq.gz	Fastqsanger.gz

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A phosphorylation-regulated eIF3d translation switch mediates cellular adaptation to metabolic stress

Project description:Shutoff of global protein synthesis is a conserved response to cellular stresses. This general phenomenon is accompanied by induction of distinct gene programs tailored to each stress condition. Although the mechanisms that lead to general repression of protein synthesis are well characterized, how cells reprogram the translation machinery for selective gene expression remains poorly understood. Here we show that the noncanonical 5′ cap-binding protein eIF3d is specifically activated in response to metabolic stress, due to loss of CK2-mediated phosphorylation near the eIF3d cap-binding pocket. Activated eIF3d controls a gene program enriched in factors important for glucose homeostasis, including members of the mTOR pathway, and eIF3d-mediated translation adaptation is essential for cell survival during chronic glucose deprivation. Our findings reveal a new mechanism of translation reprogramming engaged in response to metabolic stress.

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eIF3d controls the persistent integrated stress response

Project description:All cells respond to intrinsic and extrinsic stresses by reducing global protein synthesis and activating select gene programs necessary for survival. Here, we show the fundamental integrated stress response (ISR) is driven by the non-canonical cap-binding protein eIF3d which acts as a master effector to control core stress response orchestrators, the translation factor eIF2ɑ and the transcription factor ATF4. We find that during persistent stress, eIF3d activates translation of the protein kinase GCN2, inducing eIF2ɑ phosphorylation and inhibiting global protein synthesis. In parallel, eIF3d upregulates the m6A demethylase enzyme ALKBH5 to drive 5′ UTR-specific demethylation of stress response genes, including ATF4. Ultimately, this cascade converges on ATF4 expression by increasing mRNA engagement of translation machinery and enhancing ribosome bypass of upstream open reading frames. Our results reveal that eIF3d acts as a critical life-or-death decision point during adaptation to chronic stress and uncover a synergistic signaling mechanism in which translational cascades dynamically complement transcriptional amplification to control essential cellular processes.

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eIF4E-independent translation is largely eIF3d-dependent

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eIF4E-independent translation is largely eIF3d-dependent

Project description:We study here how mRNAs are translated in an eIF4E1-independent manner by blocking eIF4E1 using a constitutively active version of eIF4E-binding protein (4E-BP). Via ribosome profiling we identify a subset of mRNAs that are still efficiently translated when eIF4E1 is inactive. We find that these mRNAs preferentially release eIF4E1 when eIF4E1 is inactive and bind instead to eIF3D via its cap-binding pocket. eIF3D then enables these mRNAs to be efficiently translated due to its cap-binding activity.

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EIF3D Safeguards the Homeostasis of Key Signaling Pathways in Human Primed Pluripotency

Project description:Pluripotent stem cell identities such as differentiation and infinite proliferation have long been decoded in the frameworks of transcription factor networks, epigenomes, and signal transduction, yet unclear and fragmented. However, directing attention toward translation regulation, the bridge between these events promises to provide new insights into previously unexplained mechanisms. Functional screening led to the discovery that EIF3D maintains primed pluripotency via selective translation regulation. The loss of EIF3D unbalanced the pluripotency-associated signaling pathways, disrupting primed pluripotency. Furthermore, we found that EIF3D safeguards robust proliferation by managing the translation of multiple p53 regulators that maintain low p53 activity in the undifferentiated state. Therefore, this study provides a paradigm for selective translation regulation that defines the primed pluripotent stem cell identity.

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EIF3D Safeguards the Homeostasis of Key Signaling Pathways in Human Primed Pluripotency [Ribo-seq]

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EIF3D Safeguards the Homeostasis of Key Signaling Pathways in Human Primed Pluripotency [RNA-seq]

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EIF3D Safeguards the Homeostasis of Key Signaling Pathways in Human Primed Pluripotency [RNA-Seq]

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RPL12/uL11 phosphorylation regulates translation during mitosis

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