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  1. Article ; Online: A boost in learning by removing nuclear phosphodiesterases and enhancing nuclear cAMP signaling.

    Gurevich, Vsevolod V / Gurevich, Eugenia V

    Science signaling

    2023  Volume 16, Issue 778, Page(s) eadg9504

    Abstract: cAMP signaling in the nucleus leads to the expression of immediate early genes in neurons and learning and memory. In this issue ... ...

    Abstract cAMP signaling in the nucleus leads to the expression of immediate early genes in neurons and learning and memory. In this issue of
    MeSH term(s) Mice ; Animals ; Cyclic Nucleotide Phosphodiesterases, Type 4/genetics ; Cyclic Nucleotide Phosphodiesterases, Type 4/metabolism ; Signal Transduction ; Cell Nucleus/metabolism ; beta-Arrestin 2/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism
    Chemical Substances Cyclic Nucleotide Phosphodiesterases, Type 4 (EC 3.1.4.17) ; beta-Arrestin 2 ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
    Language English
    Publishing date 2023-03-28
    Publishing country United States
    Document type Journal Article ; Review ; Comment
    ZDB-ID 2417226-1
    ISSN 1937-9145 ; 1945-0877
    ISSN (online) 1937-9145
    ISSN 1945-0877
    DOI 10.1126/scisignal.adg9504
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  2. Article ; Online: Mechanisms of Arrestin-Mediated Signaling.

    Gurevich, Vsevolod V / Gurevich, Eugenia V

    Current protocols

    2023  Volume 3, Issue 6, Page(s) e821

    Abstract: Arrestins were first discovered as proteins that selectively bind active phosphorylated GPCRs and suppress (arrest) their G protein-mediated signaling. Nonvisual arrestins are also recognized as signaling proteins regulating a variety of cellular ... ...

    Abstract Arrestins were first discovered as proteins that selectively bind active phosphorylated GPCRs and suppress (arrest) their G protein-mediated signaling. Nonvisual arrestins are also recognized as signaling proteins regulating a variety of cellular pathways. Arrestins are highly flexible; they can assume many different conformations. In their receptor-bound conformation, arrestins have higher affinity for a subset of binding partners. This explains how receptor activation regulates certain branches of arrestin-dependent signaling via arrestin recruitment to GPCRs. However, free arrestins are also active molecular entities that regulate other signaling pathways and localize signaling proteins to particular subcellular compartments. Recent findings suggest that the two visuals, arrestin-1 and arrestin-4, which are expressed in photoreceptor cells, not only regulate signaling via binding to photopigments but also interact with several nonreceptor partners, critically affecting the health and survival of photoreceptor cells. Detailed in this overview are GPCR-dependent and independent modes of arrestin-mediated regulation of cellular signaling. © 2023 Wiley Periodicals LLC.
    MeSH term(s) Arrestin/metabolism ; Signal Transduction/physiology ; Arrestins/chemistry ; Arrestins/metabolism ; GTP-Binding Proteins/metabolism
    Chemical Substances Arrestin ; Arrestins ; GTP-Binding Proteins (EC 3.6.1.-)
    Language English
    Publishing date 2023-06-19
    Publishing country United States
    Document type Journal Article
    ISSN 2691-1299
    ISSN (online) 2691-1299
    DOI 10.1002/cpz1.821
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  3. Article: Location, Location, Location: The Expression of D3 Dopamine Receptors in the Nervous System.

    Gurevich, Eugenia V

    Current topics in behavioral neurosciences

    2022  

    Abstract: When the rat D3 dopamine receptor (D3R) was cloned and the distribution of its mRNA examined in 1990-1991, it attracted attention due to its peculiar distribution in the brain quite different from that of its closest relative, the D2 receptor. In the rat ...

    Abstract When the rat D3 dopamine receptor (D3R) was cloned and the distribution of its mRNA examined in 1990-1991, it attracted attention due to its peculiar distribution in the brain quite different from that of its closest relative, the D2 receptor. In the rat brain, the D3R mRNA is enriched in the limbic striatum as opposed to the D2 receptor, which is highly expressed in the motor striatal areas. Later studies in the primate and human brain confirmed relative enrichment of the D3R in the limbic striatum but also demonstrated higher abundance of the D3R in the primate as compared to the rodent brain. Additionally, in the rodent brain, the D3R in the dorsal striatum appears to be co-expressed with the D1 dopamine receptor-bearing striatal neurons giving rise to the direct output striatal pathway, although the picture is less clear with respect to the nucleus accumbens. In contrast, in the primate striatum, the D3R co-localizes with the D2 receptor throughout the basal ganglia as well as in extrastriatal brain areas. The relative abundance of the D3R in the limbic striatum, its output structures, secondary targets, and some of the other connected limbic territories may underpin its role in reward, drug dependence, and impulse control. Selective expression of D3R in the brain proliferative areas may point to its important role in the neural development as well as in neurodevelopmental abnormalities associated with schizophrenia and other developmental brain disorders.
    Language English
    Publishing date 2022-05-04
    Publishing country Germany
    Document type Journal Article
    ISSN 1866-3370
    ISSN 1866-3370
    DOI 10.1007/7854_2022_314
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  4. Article ; Online: Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins.

    Gurevich, Vsevolod V / Gurevich, Eugenia V

    International journal of molecular sciences

    2022  Volume 23, Issue 13

    Abstract: Three out of four subtypes of arrestin proteins expressed in mammals self-associate, each forming oligomers of a distinct kind. Monomers and oligomers have different subcellular localization and distinct biological functions. Here we summarize existing ... ...

    Abstract Three out of four subtypes of arrestin proteins expressed in mammals self-associate, each forming oligomers of a distinct kind. Monomers and oligomers have different subcellular localization and distinct biological functions. Here we summarize existing evidence regarding arrestin oligomerization and discuss specific functions of monomeric and oligomeric forms, although too few of the latter are known. The data on arrestins highlight biological importance of oligomerization of signaling proteins. Distinct modes of oligomerization might be an important contributing factor to the functional differences among highly homologous members of the arrestin protein family.
    MeSH term(s) Animals ; Arrestin/genetics ; Arrestin/metabolism ; Arrestins/metabolism ; Mammals/metabolism ; beta-Arrestins/metabolism
    Chemical Substances Arrestin ; Arrestins ; beta-Arrestins
    Language English
    Publishing date 2022-06-29
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms23137253
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  5. Article ; Online: Receptor-enzyme complex structures show how receptors start to switch off.

    Gurevich, Vsevolod V / Gurevich, Eugenia V

    Nature

    2021  Volume 595, Issue 7868, Page(s) 499–500

    MeSH term(s) Cell Membrane ; Multienzyme Complexes ; Signal Transduction
    Chemical Substances Multienzyme Complexes
    Language English
    Publishing date 2021-07-14
    Publishing country England
    Document type News ; Comment
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/d41586-021-01873-4
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  6. Article ; Online: Arrestin-3 binds parkin and enhances parkin-dependent mitophagy.

    Zheng, Chen / Nguyen, Kevin K / Vishnivetskiy, Sergey A / Gurevich, Vsevolod V / Gurevich, Eugenia V

    Journal of neurochemistry

    2024  

    Abstract: Arrestins were discovered for their role in homologous desensitization of G-protein-coupled receptors (GPCRs). Later non-visual arrestins were shown to regulate several signaling pathways. Some of these pathways require arrestin binding to GPCRs, the ... ...

    Abstract Arrestins were discovered for their role in homologous desensitization of G-protein-coupled receptors (GPCRs). Later non-visual arrestins were shown to regulate several signaling pathways. Some of these pathways require arrestin binding to GPCRs, the regulation of others is receptor independent. Here, we demonstrate that arrestin-3 binds the E3 ubiquitin ligase parkin via multiple sites, preferentially interacting with its RING0 domain. Identification of the parkin domains involved suggests that arrestin-3 likely relieves parkin autoinhibition and/or stabilizes the enzymatically active "open" conformation of parkin. Arrestin-3 binding enhances ubiquitination by parkin of the mitochondrial protein mitofusin-1 and facilitates parkin-mediated mitophagy in HeLa cells. Furthermore, arrestin-3 and its mutant with enhanced parkin binding rescue mitofusin-1 ubiquitination and mitophagy in the presence of the Parkinson's disease-associated R275W parkin mutant, which is defective in both functions. Thus, modulation of parkin activity via arrestin-3 might be a novel strategy of anti-parkinsonian therapy.
    Language English
    Publishing date 2024-01-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/jnc.16043
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  7. Article ; Online: Designer adhesion GPCR tells its signaling story.

    Gurevich, Eugenia V / Gurevich, Vsevolod V

    Nature chemical biology

    2020  Volume 16, Issue 12, Page(s) 1280–1281

    MeSH term(s) Receptors, G-Protein-Coupled ; Signal Transduction
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2020-08-17
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/s41589-020-00673-7
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  8. Article ; Online: Corrigendum to "Biased GPCR signaling: Possible mechanisms and inherent limitations" [Pharmacology & Therapeutics 211 (2020) 107540].

    Gurevich, Vsevolod V / Gurevich, Eugenia V

    Pharmacology & therapeutics

    2020  Volume 213, Page(s) 107615

    Language English
    Publishing date 2020-07-02
    Publishing country England
    Document type Journal Article ; Published Erratum
    ZDB-ID 194735-7
    ISSN 1879-016X ; 0163-7258
    ISSN (online) 1879-016X
    ISSN 0163-7258
    DOI 10.1016/j.pharmthera.2020.107615
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  9. Article ; Online: β

    Wess, Jürgen / Oteng, Antwi-Boasiako / Rivera-Gonzalez, Osvaldo / Gurevich, Eugenia V / Gurevich, Vsevolod V

    Pharmacological reviews

    2023  Volume 75, Issue 5, Page(s) 854–884

    Abstract: ... The ... ...

    Abstract The two
    MeSH term(s) Mice ; Animals ; beta-Arrestins/metabolism ; Arrestins/chemistry ; Arrestins/metabolism ; Signal Transduction ; Receptors, G-Protein-Coupled/metabolism ; beta-Arrestin 1/metabolism
    Chemical Substances beta-Arrestins ; Arrestins ; Receptors, G-Protein-Coupled ; beta-Arrestin 1
    Language English
    Publishing date 2023-04-07
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209898-2
    ISSN 1521-0081 ; 0031-6997
    ISSN (online) 1521-0081
    ISSN 0031-6997
    DOI 10.1124/pharmrev.121.000302
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  10. Article ; Online: GRKs as Modulators of Neurotransmitter Receptors.

    Gurevich, Eugenia V / Gurevich, Vsevolod V

    Cells

    2020  Volume 10, Issue 1

    Abstract: Many receptors for neurotransmitters, such as dopamine, norepinephrine, acetylcholine, and neuropeptides, belong to the superfamily of G protein-coupled receptors (GPCRs). A general model posits that GPCRs undergo two-step homologous desensitization: the ...

    Abstract Many receptors for neurotransmitters, such as dopamine, norepinephrine, acetylcholine, and neuropeptides, belong to the superfamily of G protein-coupled receptors (GPCRs). A general model posits that GPCRs undergo two-step homologous desensitization: the active receptor is phosphorylated by kinases of the G protein-coupled receptor kinase (GRK) family, whereupon arrestin proteins specifically bind active phosphorylated receptors, shutting down G protein-mediated signaling, facilitating receptor internalization, and initiating distinct signaling pathways via arrestin-based scaffolding. Here, we review the mechanisms of GRK-dependent regulation of neurotransmitter receptors, focusing on the diverse modes of GRK-mediated phosphorylation of receptor subtypes. The immediate signaling consequences of GRK-mediated receptor phosphorylation, such as arrestin recruitment, desensitization, and internalization/resensitization, are equally diverse, depending not only on the receptor subtype but also on phosphorylation by GRKs of select receptor residues. We discuss the signaling outcome as well as the biological and behavioral consequences of the GRK-dependent phosphorylation of neurotransmitter receptors where known.
    MeSH term(s) Animals ; Arrestins/metabolism ; G-Protein-Coupled Receptor Kinases/antagonists & inhibitors ; G-Protein-Coupled Receptor Kinases/chemistry ; G-Protein-Coupled Receptor Kinases/metabolism ; Humans ; Phosphorylation ; Receptors, G-Protein-Coupled/metabolism ; Receptors, Neurotransmitter/metabolism ; Signal Transduction/genetics
    Chemical Substances Arrestins ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter ; G-Protein-Coupled Receptor Kinases (EC 2.7.11.16)
    Language English
    Publishing date 2020-12-31
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells10010052
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