The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.
Nicotine Regulates Multiple Synaptic Proteins by Inhibiting Proteasomal Activity
Open accessAbstract
Ubiquitination regulates the degradation, membrane trafficking, and transcription of proteins. At mammalian synapses, the ubiquitin-proteasome system (UPS) influences synaptic transmission and plasticity. Nicotine also has the ability to affect synaptic function via mechanisms that remain partially unknown. We found that nicotine, at concentrations achieved by smokers, reduced proteasomal activity, produced accumulation of ubiquitinated synaptic proteins, and increased total protein levels. In particular, a 24 h exposure to nicotine decreased proteasome-dependent degradation of the alpha7 nicotinic acetylcholine receptor (nAChR) subunit, as indicated by the accumulation of ubiquitinated alpha7. The same nicotine treatment increased the levels of the AMPA glutamate receptor subunit GluR1, the NMDA receptor subunit NR2A, the metabotropic receptor mGluR1alpha, the plasticity factor Homer-1A, and the scaffolding postsynaptic density protein PSD-95, whereas the levels of another scaffolding protein, Shank, were reduced. These changes were associated with an inhibition of proteasomal chymotrypsin-like activity by nicotine. The nAChR antagonist mecamylamine was only partially able to block the effects of nicotine on the UPS, indicating that nAChR activation does not completely explain nicotine-induced inhibition of proteasomal catalytic activity. A competition binding assay suggested a direct interaction between nicotine and the 20S proteasome. These results suggest that the UPS might participate in nicotine-dependent synaptic plasticity.
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“Neuronal nAChR upregulation is an important adaptive change and a major contributor to the addictive properties of nicotine [83–86].”
From Mechanistic insights into nicotine withdrawal (2011) · cites this paper as [86]
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“Other mechanisms that likely contribute to upregulation are decreased surface receptor turnover (Peng et al. 1997) and increased receptor assembly at the endoplasmic reticulum (Corringer et al. 2006; Darsow et al. 2005; Rezvani et al. 2007, 2010; Sallette et al. 2005).”
BackgroundInfluential
Metadata
- Authors
- Rezvani, K., Teng, Y., Shim, D., & De Biasi, M.
- Affiliations
- Baylor College of Medicine (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2007-09-26
- Volume
- 27
- Issue
- 39
- Pages
- 10508-10519
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6673157
- OpenAlex
- W2027624603
- Cited by
- 113
- References
- 69
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 5 · 2021: 4 · 2020: 6 · 2019: 4 · 2018: 3 · 2017: 5 · 2016: 6 · 2015: 5 · 2014: 7 · 2013: 9 · 2012: 15
- FWCI
- 4.50
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Philip Morris International
- National Institute on Drug Abuse (DA017173, R01DA017173)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- nicotine, ubiquitin-proteasome system, proteasome inhibition, synaptic proteins, alpha7 nicotinic acetylcholine receptor, GluR1, NR2A, mGluR1alpha, Homer1a, PSD-95, shank, synaptic plasticity, chymotrypsin-like activity, mecamylamine, 20S proteasome, protein degradation
- MeSH terms
- Disks Large Homolog 4 Protein, Animals, Male, Membrane Proteins, Synaptic Transmission, Nicotine, Receptors, Nicotinic, Synapses, Protein Biosynthesis, Prefrontal Cortex, Receptors, Glutamate, Neurotransmitter Agents, Nicotinic Agonists, Models, Animal, Ubiquitin, Proteasome Endopeptidase Complex, Intracellular Signaling Peptides and Proteins, Mice, Guanylate Kinases, Proteasome Inhibitors
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