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Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [4EBP1/2]

ABSTRACT: To investigate the changes in gene expression upon loss of 4EBP1/2, we performed RNA-seq and differential gene expression analysis on WT and derived 4EBP1/2 KD cell lines. The canonical and 5′TOP mRNA cell lines used for single-molecule imaging were treated as biological replicates for the differential gene expression analysis.

ORGANISM(S): Homo sapiens

PROVIDER: GSE233182 | GEO | 2024/01/15

REPOSITORIES: GEO

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Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [LARP1]

Project description:To investigate the changes in gene expression upon loss of LARP1, we performed RNA-seq and differential gene expression analysis on WT and derived LARP1 KO cell lines. The canonical and 5′TOP mRNA cell lines used for single-molecule imaging were treated as biological replicates for the differential gene expression analysis.

2024-01-15 | GSE233183 | GEO

Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5'TOP mRNAs.

Project description:A central mechanism of mTOR complex 1 (mTORC1) signaling is the coordinated translation of ribosomal protein and translation factor mRNAs mediated by the 5'-terminal oligopyrimidine motif (5'TOP). Recently, La-related protein 1 (LARP1) was proposed to be the specific regulator of 5'TOP mRNA translation downstream of mTORC1, while eIF4E-binding proteins (4EBP1/2) were suggested to have a general role in translational repression of all transcripts. Here, we use single-molecule translation site imaging of 5'TOP and canonical mRNAs to study the translation of single mRNAs in living cells. Our data reveal that 4EBP1/2 has a dominant role in repression of translation of both 5'TOP and canonical mRNAs during pharmacological inhibition of mTOR. In contrast, we find that LARP1 selectively protects 5'TOP mRNAs from degradation in a transcriptome-wide analysis of mRNA half-lives. Our results clarify the roles of 4EBP1/2 and LARP1 in regulating 5'TOP mRNAs and provide a framework to further study how these factors control cell growth during development and disease.

| S-EPMC10871529 | biostudies-literature

Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [4EBP1/2]

Project description:Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [4EBP1/2]

| PRJNA975192 | ENA

Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [S4U label]

Project description:To investigate the changes in mRNA stablity upon loss of LARP1, we performed SLAM-seq and half-life measurements on WT and derived LARP1 KO cells. The canonical and 5′TOP mRNA cell lines used for single-molecule imaging were treated as biological replicates for the SLAM-seq analysis.

2024-01-15 | GSE233186 | GEO

Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs

Project description:This SuperSeries is composed of the SubSeries listed below.

2024-01-15 | GSE233187 | GEO

Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [LARP1]

Project description:Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [LARP1]

| PRJNA975193 | ENA

Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs

Project description:Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs

| PRJNA975195 | ENA

Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [S4U label]

Project description:Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5′TOP mRNAs [S4U label]

| PRJNA975198 | ENA

LARP1 binds ribosomes and TOP mRNAs in repressed complexes

Project description:Terminal oligopyrimidine motif-containing mRNAs (TOPs) encode all ribosomal proteins in mammals and are regulated to tune ribosome synthesis to cell state. Previous studies have implicated LARP1 in 40S- or 80S-ribosome complexes that are thought to repress and stabilize TOPs. However, a molecular understanding of how LARP1 and TOPs interact with these ribosome complexes is lacking. Here, we show that LARP1 directly binds non-translating ribosomal subunits. Cryo-EM structures reveal a previously uncharacterized domain of LARP1 bound to and occluding the mRNA channel of the 40S subunit. Increased availability of free ribosomal subunits downstream of various stresses promote 60S joining at the same interface to form LARP1-80S complexes. Simultaneously, LARP1 engages the TOP via its previously characterized La/PAM2 and DM15 domains. Contrary to expectations, ribosome binding within these complexes is not required for LARP1-mediated TOP repression or stabilization, two canonical LARP1 functions. Together, this work provides molecular insight into how LARP1 directly binds ribosomal subunits and challenges existing models describing the function of repressed LARP1-40S/80S-TOP complexes.

| S-SCDT-10_1038-S44318-024-00294-Z | biostudies-other

The LARP1 La-Module recognizes both ends of TOP mRNAs.

Project description:La-Related Protein 1 (LARP1) is an RNA-binding protein that regulates the stability and translation of mRNAs encoding the translation machinery, including ribosomal proteins and translation factors. These mRNAs are characterized by a 5'-terminal oligopyrimidine (TOP) motif that coordinates their temporal and stoichiometric expression. While LARP1 represses TOP mRNA translation via the C-terminal DM15 region, the role of the N-terminal La-Module in the recognition and translational regulation of TOP mRNAs remains elusive. Herein we show that the LARP1 La-Module also binds TOP motifs, although in a cap-independent manner. We also demonstrate that it recognizes poly(A) RNA. Further, our data reveal that the LARP1 La-Module can simultaneously engage TOP motifs and poly(A) RNA. These results evoke an intriguing molecular mechanism whereby LARP1 could regulate translation and stabilization of TOP transcripts.

| S-EPMC7927982 | biostudies-literature

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