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Arrestins: Structure, Function, and Biology
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Arrestins: Structure, Function, and Biology

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (30 June 2022) | Viewed by 10748

Special Issue Editor

Prof. Dr. Vsevolod V. Gurevich

E-Mail Website
Guest Editor
Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA
Interests: arrestin proteins; structure-function; protein engineering; GPCR signaling; GPCR trafficking; receptor regulation; cell proliferation; apoptosis; MAP kinases
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

An important challenge in biology is to understand how the information flow in numerous interconnected signalling pathways translates into a coherent cell behaviour. Cell signalling is largely regulated by protein–protein interactions, which are notoriously difficult to target with small molecules. Arrestins are a family of average-sized proteins with 3–5 members in all animals. Arrestins function as versatile adaptors, regulating the signalling by most G-protein-coupled receptors (GPCRs), of which humans express more than 800 subtypes, protein kinases, ubiquitin ligases, and other pathways, as well as GPCR trafficking. Arrestins play a role in the regulation of critical biological processes, including the function of the cardiovascular system, airways, metabolism, behaviour, the action of hormones, neurotransmitters, etc. Available structural information has revealed the role of individual arrestin elements in GPCR binding, some of which determine the receptor preference of arrestin proteins, and in arrestin transition from basal into “active” receptor-bound-like conformation. However, the identification of arrestin elements involved in their interactions with non-receptor partners, which serve as effectors in arrestin-mediated signalling, is lagging far behind. This information is vital for the design of signalling-biased arrestins that can channel the signalling of particular GPCRs to desirable pathways or away from undesirable ones.

Prof. Dr. Vsevolod V. Gurevich
Guest Editor

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

  • Arrestin
  • GPCR
  • Cell signalling
  • Receptor trafficking
  • Protein multifunctionality
  • Vision
  • Protein kinase
  • Structure–function
  • Protein engineering
  • Signalling bias

Published Papers (4 papers)

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Review

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18 pages, 1798 KiB  
Review
How Arrestins and GRKs Regulate the Function of Long Chain Fatty Acid Receptors
by Abdulrahman G. Alharbi, Andrew B. Tobin and Graeme Milligan
Int. J. Mol. Sci. 2022, 23(20), 12237; https://doi.org/10.3390/ijms232012237 - 13 Oct 2022
Cited by 1 | Viewed by 1950
Abstract
FFA1 and FFA4, two G protein-coupled receptors that are activated by long chain fatty acids, play crucial roles in mediating many biological functions in the body. As a result, these fatty acid receptors have gained considerable attention due to their potential to be [...] Read more.
FFA1 and FFA4, two G protein-coupled receptors that are activated by long chain fatty acids, play crucial roles in mediating many biological functions in the body. As a result, these fatty acid receptors have gained considerable attention due to their potential to be targeted for the treatment of type-2 diabetes. However, the relative contribution of canonical G protein-mediated signalling versus the effects of agonist-induced phosphorylation and interactions with β-arrestins have yet to be fully defined. Recently, several reports have highlighted the ability of β-arrestins and GRKs to interact with and modulate different functions of both FFA1 and FFA4, suggesting that it is indeed important to consider these interactions when studying the roles of FFA1 and FFA4 in both normal physiology and in different disease settings. Here, we discuss what is currently known and show the importance of understanding fully how β-arrestins and GRKs regulate the function of long chain fatty acid receptors. Full article
(This article belongs to the Special Issue Arrestins: Structure, Function, and Biology)
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12 pages, 3260 KiB  
Review
Scaffolding of Mitogen-Activated Protein Kinase Signaling by β-Arrestins
by Kiae Kim, Yeonjin Han, Longhan Duan and Ka Young Chung
Int. J. Mol. Sci. 2022, 23(2), 1000; https://doi.org/10.3390/ijms23021000 - 17 Jan 2022
Cited by 7 | Viewed by 2444
Abstract
β-arrestins were initially identified to desensitize and internalize G-protein-coupled receptors (GPCRs). Receptor-bound β-arrestins also initiate a second wave of signaling by scaffolding mitogen-activated protein kinase (MAPK) signaling components, MAPK kinase kinase, MAPK kinase, and MAPK. In particular, β-arrestins facilitate ERK1/2 or JNK3 activation [...] Read more.
β-arrestins were initially identified to desensitize and internalize G-protein-coupled receptors (GPCRs). Receptor-bound β-arrestins also initiate a second wave of signaling by scaffolding mitogen-activated protein kinase (MAPK) signaling components, MAPK kinase kinase, MAPK kinase, and MAPK. In particular, β-arrestins facilitate ERK1/2 or JNK3 activation by scaffolding signal cascade components such as ERK1/2-MEK1-cRaf or JNK3-MKK4/7-ASK1. Understanding the precise molecular and structural mechanisms of β-arrestin-mediated MAPK scaffolding assembly would deepen our understanding of GPCR-mediated MAPK activation and provide clues for the selective regulation of the MAPK signaling cascade for therapeutic purposes. Over the last decade, numerous research groups have attempted to understand the molecular and structural mechanisms of β-arrestin-mediated MAPK scaffolding assembly. Although not providing the complete mechanism, these efforts suggest potential binding interfaces between β-arrestins and MAPK signaling components and the mechanism for MAPK signal amplification by β-arrestin-mediated scaffolding. This review summarizes recent developments of cellular and molecular works on the scaffolding mechanism of β-arrestin for MAPK signaling cascade. Full article
(This article belongs to the Special Issue Arrestins: Structure, Function, and Biology)
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19 pages, 3190 KiB  
Review
Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors
by Preethi C. Karnam, Sergey A. Vishnivetskiy and Vsevolod V. Gurevich
Int. J. Mol. Sci. 2021, 22(22), 12481; https://doi.org/10.3390/ijms222212481 - 19 Nov 2021
Cited by 6 | Viewed by 3987
Abstract
Arrestins are a small family of proteins that bind G protein-coupled receptors (GPCRs). Arrestin binds to active phosphorylated GPCRs with higher affinity than to all other functional forms of the receptor, including inactive phosphorylated and active unphosphorylated. The selectivity of arrestins suggests that [...] Read more.
Arrestins are a small family of proteins that bind G protein-coupled receptors (GPCRs). Arrestin binds to active phosphorylated GPCRs with higher affinity than to all other functional forms of the receptor, including inactive phosphorylated and active unphosphorylated. The selectivity of arrestins suggests that they must have two sensors, which detect receptor-attached phosphates and the active receptor conformation independently. Simultaneous engagement of both sensors enables arrestin transition into a high-affinity receptor-binding state. This transition involves a global conformational rearrangement that brings additional elements of the arrestin molecule, including the middle loop, in contact with a GPCR, thereby stabilizing the complex. Here, we review structural and mutagenesis data that identify these two sensors and additional receptor-binding elements within the arrestin molecule. While most data were obtained with the arrestin-1-rhodopsin pair, the evidence suggests that all arrestins use similar mechanisms to achieve preferential binding to active phosphorylated GPCRs. Full article
(This article belongs to the Special Issue Arrestins: Structure, Function, and Biology)
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Other

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6 pages, 661 KiB  
Perspective
The Two β-Arrestins Regulate Distinct Metabolic Processes: Studies with Novel Mutant Mouse Models
by Jürgen Wess
Int. J. Mol. Sci. 2022, 23(1), 495; https://doi.org/10.3390/ijms23010495 - 02 Jan 2022
Cited by 8 | Viewed by 1638
Abstract
The two β-arrestins (β-arrestin-1 and -2; alternative names: arrestin-2 and -3, respectively) are well known for their ability to inhibit signaling via G protein-coupled receptors. However, β-arrestins can also act as signaling molecules in their own right. Although the two proteins share a [...] Read more.
The two β-arrestins (β-arrestin-1 and -2; alternative names: arrestin-2 and -3, respectively) are well known for their ability to inhibit signaling via G protein-coupled receptors. However, β-arrestins can also act as signaling molecules in their own right. Although the two proteins share a high degree of sequence and structural homology, early studies with cultured cells indicated that β-arrestin-1 and -2 are not functionally redundant. Recently, the in vivo metabolic roles of the two β-arrestins have been studied using mutant mice selectively lacking either β-arrestin-1 or -2 in cell types that are of particular relevance for regulating glucose and energy homeostasis. These studies demonstrated that the β-arrestin-1 and -2 mutant mice displayed distinct metabolic phenotypes in vivo, providing further evidence for the functional heterogeneity of these two highly versatile signaling proteins. Full article
(This article belongs to the Special Issue Arrestins: Structure, Function, and Biology)
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