Cited by 126RNA Research and SplicingGenetics and Neurodevelopmental DisordersNeuroscience and Neuropharmacology Research

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Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction

Open access

Abstract

Precise control of messenger RNA (mRNA) processing and abundance are increasingly being recognized as critical for proper spatiotemporal gene expression, particularly in neurons. These regulatory events are governed by a large number of trans-acting factors found in neurons, most notably RNA-binding proteins (RBPs) and micro-RNAs (miRs), which bind to specific cis-acting elements or structures within mRNAs. Through this binding mechanism,trans-acting factors, particularly RBPs, control all aspects of mRNA metabolism, ranging from altering the transcription rate to mediating mRNA degradation. In this context the best-characterized neuronal RBP, the Hu/ELAVl family member HuD, is emerging as a key component in multiple regulatory processes—including pre-mRNA processing, mRNA stability, and translation—governing the fate of a substantial amount of neuronal mRNAs. Through its ability to regulate mRNA metabolism of diverse groups of functionally similar genes, HuD plays important roles in neuronal development and function. Furthermore, compelling evidence indicates supplementary roles for HuD in neuronal plasticity, in particular, recovery from axonal injury, learning and memory, and multiple neurological diseases. The purpose of this review is to provide a detailed overview of the current knowledge surrounding the expression and roles of HuD in the nervous system. Additionally, we outline the present understanding of the molecular mechanisms presiding over the localization, abundance, and function of HuD in neurons.

Overview

AI snapshot

Written from the paper’s full text.

TL;DR

This review synthesizes the roles of the neuron-specific RNA-binding protein HuD/ELAVL4 in mRNA metabolism, neuronal development, plasticity, and disease. It emphasizes that HuD is a multifunctional “master regulator” whose expression and activity are controlled at transcriptional, post-transcriptional, and post-translational levels.

Key findings

  • The HuD gene spans ∼146 kb and contains seven coding exons (E2–E8) within ∼44 kb; alternative 5′ and 3′ exon use may generate up to 24 mRNA variants, and the protein is ∼40 kDa with three RNA recognition motifs (RRMs).
  • HuD binds AU-rich elements (AREs) and other U-rich motifs; less than half of HuD-bound mRNAs in one microarray screen contained an ARE, and three novel consensus motifs were present in ∼80% of HuD-targeted mRNAs in mouse forebrain.
  • HuD regulates multiple post-transcriptional steps—alternative splicing, alternative polyadenylation, nucleocytoplasmic shuttling, mRNA stability, localization, and translation—and is implicated in neuronal differentiation, neurite outgrowth, plasticity, learning/memory, nerve injury, and diseases including Alzheimer’s disease, Parkinson’s disease, spinal muscular atrophy, ALS, schizophrenia, epilepsy, and neuroendocrine cancers.
  • HuD expression/function is regulated by PKC, CARM1, AKT1, miR-375, thyroid hormone, FoxO1, and Ngn2; the review notes eight HuD exon 1 variants, with E1c predominantly expressed.

Methods

  • Narrative literature review; no primary experiments, systematic search strategy, or meta-analysis are reported.
  • Synthesizes published in vitro, cell culture, mouse, and human genetic/expression studies on HuD/ELAVL4.
  • Main analysis is descriptive integration of findings on HuD gene organization, mRNA targets, molecular functions, regulation, and disease associations.

Limitations

  • The paper is a narrative review without stated systematic review methods, inclusion criteria, or quality appraisal (evident from the text).
  • The authors state that molecular mechanisms regulating HuD expression remain incompletely understood and that further systematic investigation is needed.
  • The authors note that the precise role of HuD in some forms of neuronal plasticity requires further study.

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Integrity signals

Registry

Crossref · 10.1261/rna.039164.113

Cites

220 of 220 references verified0 citation errors · 0 not checkable

Statistics

Nothing to recompute.

Figures

FIGURE 1. Organization of the mouse HuD gene, mRNA, and protein. (A) Mouse HuD gene organization with noncoding exons depicted as orange rectangles, coding exons as gray and green rectangles, and introns as black lines. (B) Alternative splicing/processing of HuD pre-mRNA produces different HuD isoforms. 5′/3′ UTRs and coding exons are represented by orange and gray rectangles, respectively. Green rectangles denote alternatively spliced exons near the 3′ end of the gene. Also shown are the approximate locations of the Hu/ELAVl (white star), miR-375 (black star), and putative ARE (gray stars) binding sites. (C) The three major HuD protein variants found in neurons with position of RRMs (gray) and amino acid extensions in the linker region (green) shown. “P” and “Me” indicate approximate locations of serine/threonine and arginine residues that are subjected to phosphorylation by PKC and methylation by CARM1, respectively.
FIGURE 1. Organization of the mouse HuD gene, mRNA, and protein. (A) Mouse HuD gene organization with noncoding exons depicted as orange rectangles, coding exons as gray and green rectangles, and introns as black lines. (B) Alternative splicing/processing of HuD pre-mRNA produces different HuD isoforms. 5′/3′ UTRs and coding exons are represented by orange and gray rectangles, respectively. Green rectangles denote alternatively spliced exons near the 3′ end of the gene. Also shown are the approximate locations of the Hu/ELAVl (white star), miR-375 (black star), and putative ARE (gray stars) binding sites. (C) The three major HuD protein variants found in neurons with position of RRMs (gray) and amino acid extensions in the linker region (green) shown. “P” and “Me” indicate approximate locations of serine/threonine and arginine residues that are subjected to phosphorylation by PKC and methylation by CARM1, respectively.CC BY-NC · PubMed Central
FIGURE 2. Model depicting the intracellular localizations and multiple post-transcriptional functions of HuD. (A) In the nucleus, HuD regulates alternative splicing and polyadenylation by competing for specific pre-mRNA binding sites with other trans-acting factors. (B) HuD forms part of an mRNP complex, and it likely facilitates mRNA export into the cytoplasm. (C) In the cytoplasm, HuD and destabilizing RBPs bind competitively or cooperatively to mRNAs. HuD might also prevent binding of miRs to the mRNA or antagonize their function. Through these mechanisms, HuD increases the half-lives of mRNAs. (D) HuD transports mRNAs to different compartments of neurons, most notably neurites, along microtubules. (E) At the synaptic terminal, HuD may promote or repress translation of transcripts.
FIGURE 2. Model depicting the intracellular localizations and multiple post-transcriptional functions of HuD. (A) In the nucleus, HuD regulates alternative splicing and polyadenylation by competing for specific pre-mRNA binding sites with other trans-acting factors. (B) HuD forms part of an mRNP complex, and it likely facilitates mRNA export into the cytoplasm. (C) In the cytoplasm, HuD and destabilizing RBPs bind competitively or cooperatively to mRNAs. HuD might also prevent binding of miRs to the mRNA or antagonize their function. Through these mechanisms, HuD increases the half-lives of mRNAs. (D) HuD transports mRNAs to different compartments of neurons, most notably neurites, along microtubules. (E) At the synaptic terminal, HuD may promote or repress translation of transcripts.CC BY-NC · PubMed Central
FIGURE 3. Relative levels of RBPs and their cooperative and competitive binding to mRNAs controls gene expression. The relative expression of RBPs that (A,B) promote (e.g., Hu/ELAVl proteins; green) or inhibit (e.g., AUF1; red) mRNA stability/translation influences gene expression. Functionally antagonistic RBPs can also bind (C) competitively or (D,E) cooperatively to regulate mRNA fate. Cooperative binding could potentially allow for a quicker response to extracellular cues in determining mRNA fate.
FIGURE 3. Relative levels of RBPs and their cooperative and competitive binding to mRNAs controls gene expression. The relative expression of RBPs that (A,B) promote (e.g., Hu/ELAVl proteins; green) or inhibit (e.g., AUF1; red) mRNA stability/translation influences gene expression. Functionally antagonistic RBPs can also bind (C) competitively or (D,E) cooperatively to regulate mRNA fate. Cooperative binding could potentially allow for a quicker response to extracellular cues in determining mRNA fate.CC BY-NC · PubMed Central
FIGURE 4. Simplified model of the molecular events governing HuD expression, processing, and function in neurons. (A) CARM1 methylation of HuD prevents its binding to specific mRNA targets and maintains neuronal precursors in an undifferentiated state. On the other hand, an increase in unmethylated HuD protein levels, its post-translational modification (such as phosphorylation by PKC isoforms), and interaction with other proteins (e.g., AKT1) enable HuD to regulate mRNA metabolism of proneural genes and promote neuronal differentiation/neurite extension. (B) The stability and translation of mature HuD mRNA is negatively controlled by miR-375 and potentially other trans-acting factors. (C) HuD pre-mRNA undergoes alternative splicing, including inclusion of E6 mediated by Hu proteins. (D) During neuronal development transcription of the HuD gene is positively regulated by the Ngn2-E47 heterodimer binding to E-boxes upstream of E1c. Synthesis of HuD mRNA is negatively regulated by thyroid hormone (presumably bound to thyroid hormone receptor) in neurons and FoxO1 in pancreatic β cells. Green and red lines represent pathways that promote and inhibit neuronal differentiation, respectively.
FIGURE 4. Simplified model of the molecular events governing HuD expression, processing, and function in neurons. (A) CARM1 methylation of HuD prevents its binding to specific mRNA targets and maintains neuronal precursors in an undifferentiated state. On the other hand, an increase in unmethylated HuD protein levels, its post-translational modification (such as phosphorylation by PKC isoforms), and interaction with other proteins (e.g., AKT1) enable HuD to regulate mRNA metabolism of proneural genes and promote neuronal differentiation/neurite extension. (B) The stability and translation of mature HuD mRNA is negatively controlled by miR-375 and potentially other trans-acting factors. (C) HuD pre-mRNA undergoes alternative splicing, including inclusion of E6 mediated by Hu proteins. (D) During neuronal development transcription of the HuD gene is positively regulated by the Ngn2-E47 heterodimer binding to E-boxes upstream of E1c. Synthesis of HuD mRNA is negatively regulated by thyroid hormone (presumably bound to thyroid hormone receptor) in neurons and FoxO1 in pancreatic β cells. Green and red lines represent pathways that promote and inhibit neuronal differentiation, respectively.CC BY-NC · PubMed Central

Verification

Claims the paper makes

44 Partly supported · 36 No full text of the sources · 31 Sources not found · 30 Supported · 26 Own interpretation · 14 Not checked yet · 11 No basis given · 5 Supported so far · 3 Own result · 2 Mixed support · 2 Not supported · 1 Couldn’t confirm · accuracy not yet measured

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    HuD has key roles in neuronal development and plasticity and is implicated in neuronal diseases.

    “The key roles of HuD in neuronal development and plasticity and its implications in neuronal diseases raise important questions regarding the molecular mechanisms that regulate its expression.”
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Metadata

Authors
Bronicki, L. M., & Jasmin, B. J.
Affiliations
University of Ottawa (CA)
Venue
RNA
Published
2013-07-16
Volume
19
Issue
8
Pages
1019-1037
ISSN
  • 1355-8382 (ISSN-L)
  • 1469-9001
OpenAlex
W2152333262
Cited by
126
References
221
Citations by year
2026: 7 · 2025: 8 · 2024: 7 · 2023: 11 · 2022: 16 · 2021: 16 · 2020: 15 · 2019: 5 · 2018: 11 · 2017: 10 · 2016: 5 · 2015: 9 · 2014: 5 · 2013: 1
FWCI
2.69
Type
journal article
Language
en
Open access
Locations
  • RNA (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (submittedVersion, cc-by-nc)
  • PubMed Central (submittedVersion, cc-by-nc)
  • HighWire Press Open Archive (submittedVersion)
Funders
  • Muscular Dystrophy Association
  • Ontario Neurotrauma Foundation
  • Muscular Dystrophy Canada
  • Canadian Space Agency
  • Canadian Institutes of Health Research
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords
HUD, ELAVL4, RNA-binding proteins, mRNA metabolism, mRNA stability, pre-mRNA processing, translational regulation, neuronal development, neuroplasticity, learning and memory, neurological disorders, RNA localization, microRNA
MeSH terms
ELAV-Like Protein 4, Animals, Humans, Neurons, RNA, Messenger, Gene Expression Regulation, Developmental, Mice, ELAV Proteins

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