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Neuronal ELAV proteins enhance mRNA stability by a PKCα-dependent pathway

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Pascale, Alessia, Amadio, Marialaura, Scapagnini, Giovanni, Lanni, Cristina, Racchi, Marco, Provenzani, Alessandro, Govoni, Stefano, Alkon, Daniel L. +1 more·2005·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0504702102PMC PMC1189326
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Abstract

More than 1 in 20 human genes bear in the mRNA 3′ UTR a specific motif called the adenine- and uridine-rich element (ARE), which posttranscriptionally determines its expression in response to cell environmental signals. ELAV (embryonic lethal abnormal vision) proteins are the only known ARE-binding factors that are able to stabilize the bound mRNAs, thereby positively controlling gene expression. Here, we show that in human neuroblastoma SH-SY5Y cells, neuron-specific ELAV (nELAV) proteins (HuB, HuC, and HuD) are up-regulated and redistributed by 15 min of treatment with the activators of PKC phorbol esters and bryostatin-1. PKC stimulation also induces nELAV proteins to colocalize with the translocated PKCα isozyme preferentially on the cytoskeleton, with a concomitant increase of nELAV threonine phosphorylation. The same treatment promotes stabilization of growth-associated protein 43 (GAP-43) mRNA, a well known nELAV target, and induces an early increase in GAP-43 protein concentration, again only in the cytoskeletal cell fraction. Genetic or pharmacological inactivation of PKCα abolishes nELAV protein cytoskeletal up-regulation, GAP-43 mRNA stabilization, and GAP-43 protein increase, demonstrating the primary role of this specific PKC isozyme in the cascade of nELAV recruitment. Finally, in vivo PKC activation is associated with an up-regulation of nELAV proteins in the hippocampal rat brain. These findings suggest a model for gene expression regulation by nELAV proteins through a PKCα-dependent pathway that is relevant for the cellular programs in which ARE-mediated control plays a pivotal role.

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  • Stimulation of PKCα promotes its interaction with nELAV proteins, resulting in their phosphorylation at threonine residues, redistribution to neuronal cytoskeletal and membrane fractions, and stabilization of GAP-43 mRNA.

    “Moreover, stimulation of PKCα promotes its interaction with nELAV proteins resulting in their phosphorylation at threonine residues, redistribution to the neuronal cytoskeletal and membrane fractions, and stabilization of GAP-43 mRNA.”

    From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Pascale et al. 2005

    The Results report that PKC activation increases PKCα’s association with nELAV proteins and nELAV threonine phosphorylation; they also show PKCα-dependent stabilization of GAP-43 mRNA. However, the Results say the increase in nELAV proteins is confined to the cytoskeletal compartment. It is PKCα, not nELAV, that translocates to both membrane and cytoskeletal fractions (page unavailable in our copy). (LLM, conf=0.89)

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  • Various conditions, including KCl depolarization of primary hippocampal neurons, cocaine, or seizure treatment of mice and phorbol ester or bryostatin-1 application to human neuroblastoma cells, result in an augmented abundance of HuD, its redistribution to neurites, and its increased association with mRNAs and mRNP components.

    “Various conditions, including KCl depolarization of primary hippocampal neurons, cocaine, or seizure treatment of mice and phorbol ester or bryostatin-1 application to human neuroblastoma (NB) cells, result in an augmented abundance of HuD, its redistribution to neurites, and its increased association with mRNAs and mRNP components (Pascale et al. 2005; Tiruchinapalli et al. 2008a,b).”

    From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Pascale et al. 2005

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  • The classical PKCα isoform increases nELAV levels and provokes their nuclear export following treatment of SH-SY5Y NB cells with phorbol esters and bryostatin-1.

    “The classical PKCα isoform was shown to increase nELAV levels and provoke their nuclear export following treatment of SH-SY5Y NB cells with the PKC-activating compounds phorbol esters and bryostatin-1 (Pascale et al. 2005).”

    From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Pascale et al. 2005

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Authors
Pascale, A., Amadio, M., Scapagnini, G., Lanni, C., Racchi, M., Provenzani, A., Govoni, S., Alkon, D. L., & Quattrone, A.
Affiliations
Johns Hopkins University (US)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2005-08-11
Volume
102
Issue
34
Pages
12065-12070
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0504702102
PMC
PMC1189326
OpenAlex
W2044429312
Cited by
129
References
85
Citations by year
2026: 5 · 2025: 5 · 2024: 1 · 2023: 5 · 2022: 9 · 2021: 2 · 2020: 5 · 2019: 4 · 2018: 3 · 2017: 6 · 2016: 4 · 2015: 7 · 2014: 5 · 2013: 11 · 2012: 6
FWCI
3.27
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Ente Cassa di Risparmio di Firenze
  • Università degli Studi di Firenze
  • Università degli Studi di Pavia
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords
mRNA stability, protein kinase C alpha, post-transcriptional regulation, threonine phosphorylation, cytoskeleton, neuroblastoma cells, hippocampus, bryostatin 1, phorbol ester
MeSH terms
Animals, Cytoskeleton, Gene Expression Regulation, Hippocampus, Humans, Immunohistochemistry, Neurons, Phorbol Esters, RNA, Messenger, Blotting, Western, Signal Transduction, DNA Primers, Macrolides, GAP-43 Protein, Reverse Transcriptase Polymerase Chain Reaction, 3' Untranslated Regions, Amino Acid Motifs, RNA Stability, Cell Line, Tumor, Immunoprecipitation, Rats, Protein Kinase C-alpha, ELAV Proteins, Bryostatins

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