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Pumilio regulates synaptic protein function in a 3’UTR-dependent manner

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE233392 | GEO | 2025/03/03

REPOSITORIES: GEO

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Pumilio regulates synaptic protein function in a 3’ UTR-dependent manner

Project description:The regulation of RNA is crucial for spatiotemporal control of gene expression in neurons, but how the correct localization, levels, and function of synaptic proteins are achieved is not well understood. In this study, we globally investigate the role of alternative 3'UTRs in regulating RNA localization in the synaptic regions of the Drosophila brain. We identify direct mRNA targets of the translational repressor Pumilio, finding that mRNAs bound by Pumilio encode proteins enriched in synaptosomes. Pumilio differentially binds to RNA isoforms of the same gene, where shorter 3'UTRs tend to localize to the synapse, and longer 3'UTRs remain in the neuronal soma. Disruptions in 3'UTR isoform localization and axon outgrowth occur in pumilio mutant neurons. Our results reveal a mechanism of isoform-dependent protein function, demonstrating how neurons can achieve high protein complexity with a restricted set of genes.

2025-03-03 | GSE287595 | GEO

Pumilio regulates synaptic protein function in a 3’ UTR-dependent manner[primary_neuron_RNASeq]

2025-03-03 | GSE287221 | GEO

Pumilio regulates synaptic protein function in a 3’UTR-dependent manner [Synap_3seq]

2025-03-03 | GSE233391 | GEO

Pumilio regulates synaptic protein function in a 3’UTR-dependent manner [Pum_3RIPseq]

2025-03-03 | GSE233390 | GEO

Pumilio regulates synaptic protein function in a 3’ UTR-dependent manner

Project description:Pumilio regulates synaptic protein function in a 3’ UTR-dependent manner

| PRJNA1213792 | ENA

Pumilio regulates synaptic protein function in a 3’UTR-dependent manner

Project description:Pumilio regulates synaptic protein function in a 3’UTR-dependent manner

| PRJNA976181 | ENA

Pumilio regulates synaptic protein function in a 3’ UTR-dependent manner[primary_neuron_RNASeq]

Project description:Pumilio regulates synaptic protein function in a 3’ UTR-dependent manner[primary_neuron_RNASeq]

| PRJNA1211641 | ENA

Pumilio regulates synaptic protein function in a 3’UTR-dependent manner [Synap_3seq]

Project description:Pumilio regulates synaptic protein function in a 3’UTR-dependent manner [Synap_3seq]

| PRJNA976182 | ENA

Pumilio regulates synaptic protein function in a 3’UTR-dependent manner [Pum_3RIPseq]

Project description:Pumilio regulates synaptic protein function in a 3’UTR-dependent manner [Pum_3RIPseq]

| PRJNA976183 | ENA

Mammalian Pumilio 2 regulates dendrite morphogenesis and synaptic function.

Project description:In Drosophila, Pumilio (Pum) is important for neuronal homeostasis as well as learning and memory. We have recently characterized a mammalian homolog of Pum, Pum2, which is found in discrete RNA-containing particles in the somatodendritic compartment of polarized neurons. In this study, we investigated the role of Pum2 in developing and mature neurons by RNA interference. In immature neurons, loss of Pum2 led to enhanced dendritic outgrowth and arborization. In mature neurons, Pum2 down-regulation resulted in a significant reduction in dendritic spines and an increase in elongated dendritic filopodia. Furthermore, we observed an increase in excitatory synapse markers along dendritic shafts. Electrophysiological analysis of synaptic function of neurons lacking Pum2 revealed an increased miniature excitatory postsynaptic current frequency. We then identified two specific mRNAs coding for a known translational regulator, eIF4E, and for a voltage-gated sodium channel, Scn1a, which interacts with Pum2 in immunoprecipitations from brain lysates. Finally, we show that Pum2 regulates translation of the eIF4E mRNA. Taken together, our data reveal a previously undescribed role for Pum2 in dendrite morphogenesis, synapse function, and translational control.

| S-EPMC2840302 | biostudies-literature

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