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Article: Interactions between β-arrestin proteins and the cytoskeletal system, and their relevance to neurodegenerative disorders.

Szénási, Tibor / Turu, Gábor / Hunyady, László

2023 Volume 14, Page(s) 957981

Abstract: β-arrestins, which have multiple cellular functions, were initially described as proteins that desensitize rhodopsin and other G protein-coupled receptors. The cytoskeletal system plays a role in various cellular processes, including intracellular ... ...

Abstract	β-arrestins, which have multiple cellular functions, were initially described as proteins that desensitize rhodopsin and other G protein-coupled receptors. The cytoskeletal system plays a role in various cellular processes, including intracellular transport, cell division, organization of organelles, and cell cycle. The interactome of β-arrestins includes the major proteins of the three main cytoskeletal systems: tubulins for microtubules, actins for the actin filaments, and vimentin for intermediate filaments. β-arrestins bind to microtubules and regulate their activity by recruiting signaling proteins and interacting with assembly proteins that regulate the actin cytoskeleton and the intermediate filaments. Altered regulation of the cytoskeletal system plays an essential role in the development of Alzheimer's, Parkinson's and other neurodegenerative diseases. Thus, β-arrestins, which interact with the cytoskeleton, were implicated in the pathogenesis progression of these diseases and are potential targets for the treatment of neurodegenerative disorders in the future.
MeSH term(s)	Humans ; beta-Arrestins/metabolism ; Cytoskeleton/metabolism ; Microtubules/metabolism ; Actins/metabolism ; beta-Arrestin 1/metabolism ; Neurodegenerative Diseases/metabolism
Chemical Substances	beta-Arrestins ; Actins ; beta-Arrestin 1
Language	English
Publishing date	2023-02-09
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2023.957981
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Article: The Role of β-Arrestin Proteins in Organization of Signaling and Regulation of the AT1 Angiotensin Receptor.

Turu, Gábor / Balla, András / Hunyady, László

Frontiers in endocrinology

2019 Volume 10, Page(s) 519

Abstract: AT1 angiotensin receptor plays important physiological and pathophysiological roles in the cardiovascular system. Renin-angiotensin system represents a target system for drugs acting at different levels. The main effects of ATR1 stimulation involve ... ...

Abstract	AT1 angiotensin receptor plays important physiological and pathophysiological roles in the cardiovascular system. Renin-angiotensin system represents a target system for drugs acting at different levels. The main effects of ATR1 stimulation involve activation of Gq proteins and subsequent IP3, DAG, and calcium signaling. It has become evident in recent years that besides the well-known G protein pathways, AT1R also activates a parallel signaling pathway through β-arrestins. β-arrestins were originally described as proteins that desensitize G protein-coupled receptors, but they can also mediate receptor internalization and G protein-independent signaling. AT1R is one of the most studied receptors, which was used to unravel the newly recognized β-arrestin-mediated pathways. β-arrestin-mediated signaling has become one of the most studied topics in recent years in molecular pharmacology and the modulation of these pathways of the AT1R might offer new therapeutic opportunities in the near future. In this paper, we review the recent advances in the field of β-arrestin signaling of the AT1R, emphasizing its role in cardiovascular regulation and heart failure.
Language	English
Publishing date	2019-08-06
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2019.00519
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Article ; Online: An Unexpected Enzyme in Vascular Smooth Muscle Cells: Angiotensin II Upregulates Cholesterol-25-Hydroxylase Gene Expression.

Kovács, Kinga Bernadett / Szalai, Laura / Szabó, Pál / Gém, Janka Borbála / Barsi, Szilvia / Szalai, Bence / Perey-Simon, Bernadett / Turu, Gábor / Tóth, András Dávid / Várnai, Péter / Hunyady, László / Balla, András

International journal of molecular sciences

2023 Volume 24, Issue 4

Abstract: Angiotensin II (AngII) is a vasoactive peptide hormone, which, under pathological conditions, contributes to the development of cardiovascular diseases. Oxysterols, including 25-hydroxycholesterol (25-HC), the product of cholesterol-25-hydroxylase (CH25H) ...

Abstract	Angiotensin II (AngII) is a vasoactive peptide hormone, which, under pathological conditions, contributes to the development of cardiovascular diseases. Oxysterols, including 25-hydroxycholesterol (25-HC), the product of cholesterol-25-hydroxylase (CH25H), also have detrimental effects on vascular health by affecting vascular smooth muscle cells (VSMCs). We investigated AngII-induced gene expression changes in VSMCs to explore whether AngII stimulus and 25-HC production have a connection in the vasculature. RNA-sequencing revealed that
MeSH term(s)	Animals ; Rats ; Angiotensin II/metabolism ; Cells, Cultured ; Chromatography, Liquid ; Gene Expression ; Muscle, Smooth, Vascular/enzymology ; Myocytes, Smooth Muscle/metabolism ; Tandem Mass Spectrometry ; Steroid Hydroxylases/genetics
Chemical Substances	Angiotensin II (11128-99-7) ; cholesterol 25-hydroxylase (EC 1.14.99.38) ; Steroid Hydroxylases (EC 1.14.-)
Language	English
Publishing date	2023-02-16
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24043968
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Article ; Online: Novel mechanisms of G-protein-coupled receptors functions: AT

Tóth, András D / Turu, Gábor / Hunyady, László / Balla, András

Best practice & research. Clinical endocrinology & metabolism

2018 Volume 32, Issue 2, Page(s) 69–82

Abstract: ... ...

Abstract	AT
MeSH term(s)	Animals ; Humans ; Proto-Oncogene Proteins/physiology ; Receptor Cross-Talk/physiology ; Receptor, Angiotensin, Type 1/physiology ; Receptors, G-Protein-Coupled/physiology ; Signal Transduction/physiology
Chemical Substances	Proto-Oncogene Proteins ; Receptor, Angiotensin, Type 1 ; Receptors, G-Protein-Coupled ; proto-oncogene proteins c-mas-1
Language	English
Publishing date	2018-03-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2052339-7
ISSN	1878-1594 ; 1532-1908 ; 1521-690X
ISSN (online)	1878-1594 ; 1532-1908
ISSN	1521-690X
DOI	10.1016/j.beem.2018.02.003
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Article: Biased Coupling to β-Arrestin of Two Common Variants of the CB

Turu, Gábor / Soltész-Katona, Eszter / Tóth, András Dávid / Juhász, Cintia / Cserző, Miklós / Misák, Ádám / Balla, András / Caron, Marc G / Hunyady, László

Frontiers in endocrinology

2021 Volume 12, Page(s) 714561

Abstract: β-arrestins are partners of the G protein-coupled receptors (GPCRs), regulating their intracellular trafficking and signaling. Development of biased GPCR agonists, selectively targeting either G protein or β-arrestin pathways, are in the focus of ... ...

Abstract	β-arrestins are partners of the G protein-coupled receptors (GPCRs), regulating their intracellular trafficking and signaling. Development of biased GPCR agonists, selectively targeting either G protein or β-arrestin pathways, are in the focus of interest due to their therapeutic potential in different pathological conditions. The CB
MeSH term(s)	HEK293 Cells ; Humans ; Mutation, Missense ; Protein Binding ; Protein Transport ; Receptor, Cannabinoid, CB2/chemistry ; Receptor, Cannabinoid, CB2/genetics ; Receptor, Cannabinoid, CB2/metabolism ; beta-Arrestins/genetics ; beta-Arrestins/metabolism
Chemical Substances	Receptor, Cannabinoid, CB2 ; beta-Arrestins
Language	English
Publishing date	2021-08-16
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2021.714561
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Article ; Online: Impact of Medium-Sized Extracellular Vesicles on the Transduction Efficiency of Adeno-Associated Viruses in Neuronal and Primary Astrocyte Cell Cultures.

Kovács, Orsolya Tünde / Soltész-Katona, Eszter / Marton, Nikolett / Baricza, Eszter / Hunyady, László / Turu, Gábor / Nagy, György

International journal of molecular sciences

2021 Volume 22, Issue 8

Abstract: 1) Adeno-associated viruses (AAV) are safe and efficient gene therapy vectors with promising results in the treatment of several diseases. Extracellular vesicles (EV) are phospholipid bilayer-surrounded structures carrying several types of lipids, ... ...

Abstract	(1) Adeno-associated viruses (AAV) are safe and efficient gene therapy vectors with promising results in the treatment of several diseases. Extracellular vesicles (EV) are phospholipid bilayer-surrounded structures carrying several types of lipids, proteins, and nucleic acids with the ability to cross biological barriers. EV-associated AAVs might serve as new and efficient gene therapy vectors considering that they carry the benefits of both AAVs and EVs. (2) We tested vesicle-associated AAVs and vesicles mixed with AAVs on two major cell types of the central nervous system: a neural cell line (N2A) and primary astrocyte cells. (3) In contrast to previously published in vivo observations, the extracellular vesicle packaging did not improve but, in the case of primary astrocyte cells, even inhibited the infection capacity of the AAV particles. The observed effect was not due to the inhibitory effects of the vesicles themselves, since mixing the AAVs with extracellular vesicles did not change the effectiveness. (4) Our results suggest that improvement of the in vivo efficacy of the EV-associated AAV particles is not due to the enhanced interaction between the AAV and the target cells, but most likely to the improved delivery of the AAVs through tissue barriers and to the shielding of AAVs from neutralizing antibodies.
MeSH term(s)	Animals ; Astrocytes/metabolism ; Cell Line ; Cells, Cultured ; Dependovirus/metabolism ; Extracellular Vesicles/metabolism ; Genetic Vectors/genetics ; Humans ; Transduction, Genetic/methods
Language	English
Publishing date	2021-04-19
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22084221
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Article ; Online: A general method for quantifying ligand binding to unmodified receptors using Gaussia luciferase.

Tóth, András Dávid / Garger, Dániel / Prokop, Susanne / Soltész-Katona, Eszter / Várnai, Péter / Balla, András / Turu, Gábor / Hunyady, László

The Journal of biological chemistry

2021 Volume 296, Page(s) 100366

Abstract: Reliable measurement of ligand binding to cell surface receptors is of outstanding biological and pharmacological importance. Resonance energy transfer-based assays are powerful approaches to achieve this goal, but the currently available methods are ... ...

Abstract	Reliable measurement of ligand binding to cell surface receptors is of outstanding biological and pharmacological importance. Resonance energy transfer-based assays are powerful approaches to achieve this goal, but the currently available methods are hindered by the necessity of receptor tagging, which can potentially alter ligand binding properties. Therefore, we developed a tag-free system to measure ligand‒receptor interactions in live cells using the Gaussia luciferase (GLuc) as a bioluminescence resonance energy transfer donor. GLuc is as small as the commonly applied Nanoluciferase but has enhanced brightness, and its proper substrate is the frequently used coelenterazine. In our assay, bystander bioluminescence resonance energy transfer is detected between a GLuc-based extracellular surface biosensor and fluorescent ligands bound to their unmodified receptors. The broad spectrum of applications includes equilibrium and kinetic ligand binding measurements for both labeled and competitive unlabeled ligands, and the assay can be utilized for different classes of plasma membrane receptors. Furthermore, the assay is suitable for high-throughput screening, as evidenced by the identification of novel α
MeSH term(s)	Biological Assay ; Bioluminescence Resonance Energy Transfer Techniques/methods ; Cell Membrane/metabolism ; Energy Transfer ; HEK293 Cells ; Humans ; Kinetics ; Ligands ; Luciferases/chemistry ; Luciferases/metabolism ; Protein Binding ; Protein Transport ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction
Chemical Substances	Ligands ; Receptors, G-Protein-Coupled ; Luciferases (EC 1.13.12.-)
Language	English
Publishing date	2021-02-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100366
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Article: Functional Rescue of a Nephrogenic Diabetes Insipidus Causing Mutation in the V2 Vasopressin Receptor by Specific Antagonist and Agonist Pharmacochaperones.

Szalai, Laura / Sziráki, András / Erdélyi, László Sándor / Kovács, Kinga Bernadett / Tóth, Miklós / Tóth, András Dávid / Turu, Gábor / Bonnet, Dominique / Mouillac, Bernard / Hunyady, László / Balla, András

Frontiers in pharmacology

2022 Volume 13, Page(s) 811836

Abstract: The urine concentrating function of the kidney is essential to maintain the water homeostasis of the human body. It is mainly regulated by the arginine-vasopressin (AVP), which targets the type 2 vasopressin receptor (V2R) in the kidney. The inability of ...

Abstract	The urine concentrating function of the kidney is essential to maintain the water homeostasis of the human body. It is mainly regulated by the arginine-vasopressin (AVP), which targets the type 2 vasopressin receptor (V2R) in the kidney. The inability of V2R to respond to AVP stimulation leads to decreased urine concentration and congenital nephrogenic diabetes insipidus (NDI). NDI is characterized by polyuria, polydipsia, and hyposthenuria. In this study, we identified a point mutation (S127F) in the
Language	English
Publishing date	2022-01-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587355-6
ISSN	1663-9812
ISSN	1663-9812
DOI	10.3389/fphar.2022.811836
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Article ; Online: Proteomic Changes of Osteoclast Differentiation in Rheumatoid and Psoriatic Arthritis Reveal Functional Differences.

Kovács, Orsolya Tünde / Tóth, Eszter / Ozohanics, Olivér / Soltész-Katona, Eszter / Marton, Nikolett / Buzás, Edit Irén / Hunyady, László / Drahos, László / Turu, Gábor / Nagy, György

Frontiers in immunology

2022 Volume 13, Page(s) 892970

Abstract: Background: Osteoclasts play a crucial role in the maintenance, repair, and remodeling of bones of the adult vertebral skeleton due to their bone resorption capability. Rheumatoid arthritis (RA) and psoriatic arthritis (PsA) are associated with ... ...

Abstract	Background: Osteoclasts play a crucial role in the maintenance, repair, and remodeling of bones of the adult vertebral skeleton due to their bone resorption capability. Rheumatoid arthritis (RA) and psoriatic arthritis (PsA) are associated with increased activity of osteoclasts. Objectives: Our study aimed to investigate the dynamic proteomic changes during osteoclast differentiation in healthy donors, in RA, and PsA. Methods: Blood samples of healthy donors, RA, and PsA patients were collected, and monocytes were isolated and differentiated into osteoclasts Results: The analysis of the proteomic changes revealed that during the differentiation of the human osteoclasts, expression of the proteins involved in metabolic activity, secretory function, and cell polarity is increased; by contrast, signaling pathways involved in the immune functions are downregulated. Interestingly, the differences between cells of healthy donors and RA/PsA patients are most pronounced after the final steps of differentiation to osteoclasts. In addition, both in RA and PsA the differentiation is characterized by decreased metabolic activity, associated with various immune pathway activities; furthermore by accelerated cytokine production in RA. Conclusions: Our results shed light on the characteristic proteomic changes during human osteoclast differentiation and expression differences in RA and PsA, which reveal important pathophysiological insights in both diseases.
MeSH term(s)	Adult ; Arthritis, Psoriatic ; Arthritis, Rheumatoid ; Bone Resorption ; Humans ; Osteoclasts/metabolism ; Proteomics
Language	English
Publishing date	2022-07-04
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2022.892970
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Article ; Online: Signal transduction of the CB1 cannabinoid receptor.

Turu, Gábor / Hunyady, László

Journal of molecular endocrinology

2010 Volume 44, Issue 2, Page(s) 75–85

Abstract: The CB(1) cannabinoid receptor (CB(1)R) is the major cannabinoid receptor in neuronal cells and the brain, but it also occurs in endocrine cells and other peripheral tissues. CB(1)R is a member of the superfamily of G-protein-coupled receptors (GPCRs), ... ...

Abstract	The CB(1) cannabinoid receptor (CB(1)R) is the major cannabinoid receptor in neuronal cells and the brain, but it also occurs in endocrine cells and other peripheral tissues. CB(1)R is a member of the superfamily of G-protein-coupled receptors (GPCRs), which are characterized by seven transmembrane helices. The major mediators of CB(1)R are the G proteins of the G(i/o) family, which inhibit adenylyl cyclases in most tissues and cells, and regulate ion channels, including calcium and potassium ion channels. Regulation of ion channels is an important component of neurotransmission modulation by endogenous cannabinoid compounds released in response to depolarization and Ca(2+)-mobilizing hormones. However, evidence exists that CB(1)Rs can also stimulate adenylyl cyclase via G(s), induce receptor-mediated Ca(2+) fluxes and stimulate phospholipases in some experimental models. Stimulation of CB(1)R also leads to phosphorylation and activation of mitogen-activated protein kinases (MAPK), such as p42/p44 MAPK, p38 MAPK and c-Jun N-terminal kinase, which can regulate nuclear transcription factors. Activated and phosphorylated CB(1)Rs also associate with beta-arrestin molecules, which can induce the formation of signalling complexes and participate in the regulation of GPCR signalling. Recent data also suggest that CB(1)Rs can form homo- and heterodimers/oligomers, and the altered pharmacological properties of these receptor complexes may explain the pharmacological differences observed in various tissues.
MeSH term(s)	Animals ; Humans ; Receptor, Cannabinoid, CB1/metabolism ; Signal Transduction
Chemical Substances	Receptor, Cannabinoid, CB1
Language	English
Publishing date	2010-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	645012-x
ISSN	1479-6813 ; 0952-5041
ISSN (online)	1479-6813
ISSN	0952-5041
DOI	10.1677/JME-08-0190
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