Structural Mechanism of the Arrestin-3/JNK3 Interaction

Park, Ji Young; Qu, Changxiu; Li, Rui-Rui; Yang, Fan; Yu, Xiao; Shen, Yuemao; Cai, Bo-yang; Yun, Youngjoo; Sun, Junying; Chung, Ka Young

doi:10.1016/j.str.2019.04.002

Cited by 20 publications

(21 citation statements)

References 52 publications

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“…4A). 51 The fidelity of SeF incorporation was confirmed by SDS-PAGE, and Bodipy593 labeling was easily detected by gel imaging (Fig. 2D).…”

Section: Monitoring Conformational Changes Of βArr1 Activated Bymentioning

confidence: 76%

“…Our recent results have suggested that the β-1 strand is one of the functional motifs in mediating JNK3 activation downstream of β-arrestins. 51 We therefore selected the T6 in the β-1 strand of arrestin and incorporated the Bodipy593 at this site to examine how receptor binding triggers arrestin conformational change. We selected two labeling sites for smFRET, the T6 site and the L191 position, whose relative distance undergoes a 7 Å change (from 63 Å to 70 Å ) (Table S7 †) during the activation process of the arrestin.…”

Section: Chemical Science Accepted Manuscriptmentioning

confidence: 99%

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Single-molecule FRET and conformational analysis of beta-arrestin-1 through genetic code expansion and a Se-click reaction

Han

Yang

et al. 2021

Chem. Sci.

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“…4A). 51 The fidelity of SeF incorporation was confirmed by SDS-PAGE, and Bodipy593 labeling was easily detected by gel imaging (Fig. 2D).…”

Section: Monitoring Conformational Changes Of βArr1 Activated Bymentioning

confidence: 76%

Section: Chemical Science Accepted Manuscriptmentioning

confidence: 99%

Single-molecule FRET and conformational analysis of beta-arrestin-1 through genetic code expansion and a Se-click reaction

Han

Yang

et al. 2021

Chem. Sci.

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“…By examining the changes in chemical shift induced by the binding of distinctly phosphorylated peptides, they showed that phosphorylation patterns generated by different GPCR kinases induce at least three active conformations of arr that are coupled to distinct downstream interaction partners. The ncAA F2Y was employed also by Park et al to probe the interaction interface between barr-2 and the MAPK c-Jun N-terminal kinase 3 [129]. They identified the first b-sheet of the barr-2 N-domain as key element for the interaction.…”

Section: In Vitro Probes To Dissect the Mechanism Of Arrestin Bindingmentioning

confidence: 99%

“…The ncAA F2Y was employed also by Park et al . to probe the interaction interface between βarr‐2 and the MAPK c‐Jun N‐terminal kinase 3 [129]. They identified the first β‐sheet of the βarr‐2 N‐domain as key element for the interaction.…”

Section: In Vitro Probes To Dissect the Mechanism Of Arrestin Bindingmentioning

confidence: 99%

Biochemical insights into structure and function of arrestins

Aydin

Coin

2021

The FEBS Journal

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Arrestins (arr) are multifunctional cytosolic adaptors that bind to active and phosphorylated G protein-coupled receptors (GPCRs) via a highly versatile interface. Arrestins stop G protein signaling and trigger other signaling pathways. Recently, 3D structures of arr-GPCR complexes have been solved, which provide a bulk of structural information for understanding the mechanism of arr recruitment and activation. However, many questions about the functional consequences of structural details and the dynamics of the arr-GPCR interaction remain open. A wealth of information about key determinants for the arr-GPCR interaction and their functional relevance, and dynamic insights into the process of arr binding and the functional outcomes of different binding modes have been provided by a series of biochemical methods which we review here. Importantly, most of these methods provide information from the live cell, which is a necessary validation and complement for structural data. With the main focus on the most recent research, we will highlight major findings about arr structure, function, and dynamics derived from mutagenesis studies, cross-linking studies, conformational probes, and sensors, and we summarize available systems to detect arr recruitment. Furthermore, we discuss recent findings and directions of in silico investigations in arr-GPCR complexes.

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“…C-lobe regions near the activation loop of JNK3 form a potential binding interface, which varies depending on ATP binding status. Because the β1 strand of β-arrestin 2 is covered by the C-terminal strand in its basal state, C-terminal truncation (i.e., pre-activation) of β-arrestin 2 facilitates the β-arrestin 2/JNK3 interaction [ 64 ].…”

Section: Biological Properties Of Jnk3mentioning

confidence: 99%

Biological Properties of JNK3 and Its Function in Neurons, Astrocytes, Pancreatic β-Cells and Cardiovascular Cells

Nakano

Nakayama

Saito

2020

Cells

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JNK is a protein kinase, which induces transactivation of c-jun. The three isoforms of JNK, JNK1, JNK2, and JNK3, are encoded by three distinct genes. JNK1 and JNK2 are expressed ubiquitously throughout the body. By contrast, the expression of JNK3 is limited and observed mainly in the brain, heart, and testes. Concerning the biological properties of JNKs, the contribution of upstream regulators and scaffold proteins plays an important role in the activation of JNKs. Since JNK signaling has been described as a form of stress-response signaling, the contribution of JNK3 to pathophysiological events, such as stress response or cell death including apoptosis, has been well studied. However, JNK3 also regulates the physiological functions of neurons and non-neuronal cells, such as development, regeneration, and differentiation/reprogramming. In this review, we shed light on the physiological functions of JNK3. In addition, we summarize recent advances in the knowledge regarding interactions between JNK3 and cellular reprogramming.

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Structural Mechanism of the Arrestin-3/JNK3 Interaction

Cited by 20 publications

References 52 publications

Single-molecule FRET and conformational analysis of beta-arrestin-1 through genetic code expansion and a Se-click reaction

Single-molecule FRET and conformational analysis of beta-arrestin-1 through genetic code expansion and a Se-click reaction

Biochemical insights into structure and function of arrestins

Biological Properties of JNK3 and Its Function in Neurons, Astrocytes, Pancreatic β-Cells and Cardiovascular Cells

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