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RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression [PAR_Clip-seq]

ABSTRACT: RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression [PAR_Clip-seq]

PROVIDER: PRJNA908728 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR22526251.fastq.gz	Fastqsanger.gz
	SRR22526252.fastq.gz	Fastqsanger.gz
	SRR22526253.fastq.gz	Fastqsanger.gz
	SRR22526254.fastq.gz	Fastqsanger.gz

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Similar Datasets

RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression [PAR_Clip-seq]

Project description:Accumulating evidence suggests that posttranscriptional regulation of gene expression, including regulation of RNA splicing, transport, modification, translation, and degradation, primarily relies on RNA binding proteins (RBPs). However, the functions of many RBPs remain understudied. Here, we characterized the function of a novel RBP, Proline-Rich Coiled-coil 2B (PRRC2B). Through photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation (PAR-CLIP) and deep sequencing, we identified transcriptome-wide CU- or GA-rich PRRC2B binding sites around the translation initiation codon on a specific cohort of mRNAs in HEK293T cells. These PRRC2B target mRNAs, including oncogenes and cell cycle regulators such as CCND2 (cyclin D2), exhibited decreased translation upon PRRC2B knockdown as revealed by sequencing polysome-associated RNA, resulting in decreased G1/S phase transition and cell proliferation. Antisense oligonucleotides (ASOs) blocking PRRC2B-CCND2 mRNA interaction decreased CCND2 translation, thus inhibited G1/S transition and cell proliferation. Mechanistically, PRRC2B interactome capture analysis revealed RNA-independent interactions with eukaryotic initiation factors eIF4G2, eIF3, and FXR1. The interaction with eIF4G2 is essential for PRRC2B function since unlike wildtype PRRC2B, eIF4G2-interacting defective mutants failed to rescue the translation deficiency caused by PRRC2B knockdown. Taken together, our findings reveal that PRRC2B, by interacting with eIF4G2, is essential for efficient translation of specific proteins required for cell cycle progression and cell proliferation.

2023-04-20 | GSE220057 | GEO

RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression [Polysome-seq]

2023-04-20 | GSE220058 | GEO

RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression

Project description:RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression

| PRJNA908730 | ENA

RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression [Polysome-seq]

Project description:RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression [Polysome-seq]

| PRJNA908733 | ENA

The RNA-binding protein PRRC2B preserves 5' TOP mRNA during starvation to maintain ribosome biogenesis during recovery

Project description:PRRC2B is an intrinsically disordered RNA-binding protein that is part of the cell’s translation machinery. Here we show that PRRC2B has two alternatively spliced mRNA transcripts producing major long and minor short isoforms. Mass spectrometry-based interaction studies indicated that both isoforms associate with the 40S ribosomal subunit and translation initiation factors. Importantly, the long isoform also interacted with additional RNA-binding proteins through its unique Arg/Gly-rich region. Among these is LARP1, a regulator of 5' TOP mRNAs under conditions of mTOR inhibition. We discovered that like LARP1, PRRC2B is an important regulator of 5' TOP mRNA levels during starvation, particularly those encoding ribosomal proteins. Overall, our study elucidates a newly discovered function for PRRC2B as an RNA-binding protein that regulates ribosomal biogenesis, establishing it as a global regulator of translation in addition to its function in initiating specific target translation.

2025-10-26 | GSE282113 | GEO

RNA binding protein PRRC2B mediates translation of specific mRNAs and regulates cell cycle progression.

Project description:Accumulating evidence suggests that posttranscriptional control of gene expression, including RNA splicing, transport, modification, translation and degradation, primarily relies on RNA binding proteins (RBPs). However, the functions of many RBPs remain understudied. Here, we characterized the function of a novel RBP, Proline-Rich Coiled-coil 2B (PRRC2B). Through photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation and sequencing (PAR-CLIP-seq), we identified transcriptome-wide CU- or GA-rich PRRC2B binding sites near the translation initiation codon on a specific cohort of mRNAs in HEK293T cells. These mRNAs, including oncogenes and cell cycle regulators such as CCND2 (cyclin D2), exhibited decreased translation upon PRRC2B knockdown as revealed by polysome-associated RNA-seq, resulting in reduced G1/S phase transition and cell proliferation. Antisense oligonucleotides blocking PRRC2B interactions with CCND2 mRNA decreased its translation, thus inhibiting G1/S transition and cell proliferation. Mechanistically, PRRC2B interactome analysis revealed RNA-independent interactions with eukaryotic translation initiation factors 3 (eIF3) and 4G2 (eIF4G2). The interaction with translation initiation factors is essential for PRRC2B function since the eIF3/eIF4G2-interacting defective mutant, unlike wild-type PRRC2B, failed to rescue the translation deficiency or cell proliferation inhibition caused by PRRC2B knockdown. Altogether, our findings reveal that PRRC2B is essential for efficiently translating specific proteins required for cell cycle progression and cell proliferation.

| S-EPMC10287950 | biostudies-literature

The binding RNAs of Prrc2b in brain tissues of Prrc2b-HA knock-in mice [RIP-Seq]

Project description:We performed HA RIP-seq in cerebral cortexes of WT and Prrc2b-HA knockin mice at P4 to further analyze genes that Prrc2b selectively binds.

2025-09-15 | GSE243309 | GEO

PRRC2 proteins are translation factors that promote leaky scanning

Project description:Most animal mRNAs contain upstream Open Reading Frames (uORFs). These uORFs represent an impediment to translation of the main ORF since ribosomes usually bind the mRNA cap at the 5’ end and then scan for ORFs in a 5’-to-3’ fashion. One way for ribosomes to bypass uORFs is via leaky scanning, whereby the ribosome disregards the uORF start codon. Hence leaky scanning is an important post-transcriptional mechanism affecting gene expression. Few molecular factors regulating or facilitating this process are known. Here we identify the PRRC2 proteins PRRC2A, PRRC2B and PRRC2C as translation initiation factors. We find that they bind other eukaryotic translation initiation factors and preinitiation complexes and are enriched on ribosomes translating mRNAs with uORFs. We find that PRRC2 proteins promote translation of mRNAs containing uORFs by facilitating leaky scanning past uORFs. Since PRRC2 proteins have been associated with cancer, this provides a mechanistic starting point for understanding their physiological and pathophysiological roles.

2023-02-11 | GSE211440 | GEO

RNA binding protein PRRC2B mediates translation of specific proteins and regulates cell cycle progression

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

2023-04-20 | GSE220059 | GEO

Identification of human PRRC2B isoform interactors

Project description:Two isoforms (Long isoform ~220 KDa, short isoform ~150 KDa) of the human PRRC2B protein (Uniprot accession Q5JSZ5) were recombinantly expressed with an HA-tag in HEK293 cell lines. The goal of the experiment is to identify differential interactors of the short vs long isoforms, in addition to their common interactors. To this aim, 3 sample types were analyzed by IP-MS: HA-tagged long PRRC2B, HA-tagged short PRRC2B, and HA-tagged mCherry (control). Four biological replicates were analyzed from each experimental group.

2025-10-26 | PXD057527 | Pride

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