Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The RNA binding protein HNRNPA2B1 regulates RNA abundance and motor protein activity in neurites

ABSTRACT: RNA molecules are localized to subcellular regions through interactions between localization-regulatory cis-elements and trans-acting RNA binding proteins (RBPs). However, the identities of RNAs whose localization is regulated by a specific RBP as well as the impacts of that RNA localization on cell function have generally remained unknown. Here, we demonstrate that the RBP HNRNPA2B1 acts to keep specific RNAs out of neuronal projections. Using subcellular fractionation, high-throughput sequencing, and single molecule RNA FISH, we find that hundreds of RNAs demonstrate markedly increased abundance in neurites in HNRNPA2B1 knockout cells. These RNAs often encode motor proteins and are enriched for known HNRNPA2B1 binding sites and motifs in their 3′ UTRs. The speed and processivity of microtubule-based transport is impaired in these cells, specifically in their neurites. HNRNPA2B1 point mutations that increase its cytoplasmic abundance relative to wildtype lead to stronger suppression of both RNA mislocalization and transport defects than seen with wildtype HNRNPA2B1. We further find that the subcellular localizations of HNRNPA2B1 target RNAs are sensitive to perturbations of RNA decay machinery, suggesting that it is HNRNPA2B1’s known role in regulating RNA stability that may explain these observations. These findings establish HNRNPA2B1 as a negative regulator of neurite RNA abundance and link the subcellular activities of motor proteins with the subcellular abundance of the RNAs that encode them.

ORGANISM(S): Mus musculus

PROVIDER: GSE275212 | GEO | 2024/08/20

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

The RNA binding protein HNRNPA2B1 regulates RNA abundance and motor protein activity in neurites

Project description:The RNA binding protein HNRNPA2B1 regulates RNA abundance and motor protein activity in neurites

| PRJNA1149810 | ENA

RNA-seq of neuronal compartments with perturbed mRNA degradation machinery

Project description:We have perturbed mRNA degradation machinery and investigated the change in subcellular localization of mRNA in Ascl1-induced neurons (iNeurons). Mutant iNeuron line harbouring a ponasteroneA-inducible heterozygous dominant-negative Caf1 (dnCaf1) was generated, separated into neuronal compartments (soma and neurites) and sequenced in parallel with compartments from the Wild Type iNeurons (WT). Differential localization of mRNA between soma and neurites in the WT was then compared to the localization in dnCaf1 in order to identify the changes in localization.

2023-12-31 | E-MTAB-9398 | biostudies-arrayexpress

Subcellular refinement of RNA binding protein target interactions with colocalization CLIP [RNA-seq]

Project description:RNA binding proteins (RBPs) are essential for RNA metabolism and have profound impacts in both health and disease. The subcellular organization of RBP interaction networks with target RNAs remains largely unexplored. Here, we develop colocalization CLIP, a method that combines CrossLinking and ImmunoPrecipitation (CLIP) with proximity labeling, to explore in-depth the subcellular RNA interactions of the well-studied RNA-binding protein HuR. Using this method, we uncover HuR's dynamic and location-specific interactions with RNA, revealing alterations in sequence preferences and interactions in the nucleus, cytosol, or stress granule compartments. We uncover HuR's unique binding preferences within stress granules during arsenite stress, illuminating intricate interactions that conventional methodologies cannot capture. Overall, coCLIP provides a powerful method for revealing RBP:RNA interactions based on localization, and lays the foundation for an advanced understanding of RBP models that incorporate subcellular location as a critical determinant of their functions.

2023-10-25 | GSE245210 | GEO

Subcellular refinement of RNA binding protein target interactions with colocalization CLIP [CLIP-seq]

2023-10-25 | GSE245209 | GEO

Systematic analysis of the impact of R-methylation on RBPs-RNA interactions

Project description:RNA binding proteins (RBPs) bind RNAs through specific RNA-binding domains, generating multi-molecular complexes known as ribonucleoproteins (RNPs). Various post-translational modifications (PTMs) have been described to regulate RBP structure, subcellular localization and interactions with other proteins or RNAs. Recent proteome-wide experiments showed that RBPs are the most representative group within the class of arginine (R)-methylated proteins; moreover, emerging evidence suggests that this modification plays a major role in the regulation of RBP-RNA interaction. Nevertheless, a systematic analysis of how changes in protein-R-methylation can affect globally RBPs-RNA interactions has not yet been carried out. We describe here a quantitative proteomics approach to profile global changes of RBP-RNA interactions upon the modulation of protein arginine methyltransferases PRMT1 and PRMT5. By coupling the recently described Orthogonal Organic Phase Separation (OOPS) with SILAC labelling and pharmacological modulation of PRMT1 and PRMT5 enzyme, we describe the RNA-binding protein dynamics in dependence of protein-R-methylation.

2021-08-25 | PXD024601 | Pride

Sequencing of a human Orfeome in subcellular compartments of mouse primary cortical neurons (mPCN)

Project description:To study how the codon composition of the coding sequence affects subcellular localization of mRNA in an unbiased way, mouse primary cortical neurons were transfected with a collection of human open reading frames (ORFs) with identical untranslated regions, separated into soma and neurites, and subjected to RNA sequencing with specific amplification of the ORFs.

2023-07-12 | E-MTAB-11571 | biostudies-arrayexpress

RNA localization is a key determinant of neurite-enriched proteome

Project description:RNA localization and local translation are important biological processes that underlie establishment of body axis, cell migration and synaptic plasticity. However, it is unclear to which extent mRNA localization contributes toward local proteome and how much of protein localization is achieved via protein transport or local translation of uniformly distributed mRNAs. To address this question, we performed genome-wide analysis of the local proteome, transcriptome, and translation rates in neurites and cell bodies of neurons differentiated from mouse embryonic stem cells. Our results reveal mRNA localization as a key determinant of protein localization to neurites that accounts for around a half of the neurite-localized proteome. Moreover, we identify non-coding RNAs and RNA-binding proteins targeted to neurites.

2018-06-06 | PXD004640 | Pride

RNA localization is a key determinant of neurite-enriched proteome, fractionation samples

2018-06-06 | PXD004751 | Pride

Sumoylated hnrnpa2b1 controls the sorting of miRNAs into two exosomes through binding to specific motifs

Project description:Exosomes are released by most cells to the extracellular environment, and are involved in cell-to-cell-communication. Exosomes contain specific repertoires of mRNAs, miRNAs and other non-coding RNAs that can be functionally transferred to recipient cells. However, the mechanisms that control the specific loading of RNA species into exosomes remain unknown. Here we describe short sequence motifs present in miRNAs that control their localization into exosomes. The protein hnRNPA2B1 specifically binds exosomal miRNAs through the recognition of these motifs and controls their loading into exosomes. Moreover, hnRNPA2B1 in exosomes is sumoylated, and sumoylation controls the binding of hnRNPA2B1 to miRNAs. The loading of miRNAs into exosomes can be modulated by mutagenesis of the identified motifs or changes in hnRNPA2B1 expression levels. These findings identify hnRNPA2B1 as a key player in miRNA sorting into exosomes and provide potential tools for the packaging of selected regulatory RNAs into exosomes and their use in biomedical applications.

2014-04-16 | PXD000350 | Pride

Muscleblind-like proteins use modular domains to localize RNAs by riding kinesins and docking to membranes

Project description:RNA transport and local translation provide spatial control of gene expression, and RNA binding proteins (RBPs) act as critical adapters in this multi-step process. Muscleblind-like (MBNL) RNA binding proteins, implicated in Myotonic Dystrophy and cancer, localize RNAs to myoblast membranes and distal neurites, through unknown mechanisms. We found that MBNLs form motile and anchored granules in neurons and myoblasts, and selectively associate with kinesins Kif1bα and Kif1c through its zinc finger (ZnF) domains. Other RBPs with similar ZnFs also associate with these kinesins, implicating a motor-RBP specificity code. Live cell imaging and fractionation revealed that membrane anchoring is mediated through the unstructured carboxy-terminal tail of MBNL1. Both kinesin- and membrane-recruitment functions were reconstituted using MBNL-MS2 coat protein fusions; this approach, termed RBP Module Recruitment and Imaging (RBP-MRI), decouples RNA binding, kinesin recruitment, and membrane anchoring functions, while also establishing general strategies for studying multi-functional, modular domains of RBPs.

2022-07-09 | GSE207597 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data