The Two Non-Visual Arrestins Engage ERK2 Differently

Perry-Hauser, Nicole A.; Hopkins, Jesse B.; Zhuo, Ya; Chen, Zheng; Perez, Ivette; Schultz, Kathryn M.; Vishnivetskiy, Sergey A.; Kaya, Ali I.; Sharma, Pankaj; Dalby, Kevin N.; Chung, Ka Young; Klug, Candice S.; Gurevich, Vsevolod V.; Iverson, T.M.

doi:10.1016/j.jmb.2022.167465

Cited by 15 publications

(10 citation statements)

References 84 publications

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“…Cellular investigations implicate the barr C tail in internalization as well as signaling processes downstream of receptor engagement (Gurevich and Gurevich, 2015;Perry-Hauser et al, 2022). When barr is activated, its C tail may sample an ensemble of positions on a sub-millisecond timescale or adopt a more limited set of positions that are partially stabilized by residual contacts with the barr N-and C-terminal domains.…”

Section: Discussionmentioning

confidence: 99%

“…The position and conformation of the barr tail in the active state are not known, as the entire barr tail is either removed or unresolved in these structures (Gurevich et al, 2018). The barr tail contains regions that bind clathrin and adaptin, and it may also be directly involved in, or expose N-domain regions important for, scaffolding signaling kinases, including a direct interaction with extracellular signal-regulated kinase 2 (Gurevich and Gurevich, 2015;Perry-Hauser et al, 2022). Thus, the timing and nature of barr tail release, as it relates to receptor engagement and other structural rearrangements in barr, are critical for understanding barr-mediated signaling.…”

Section: Introductionmentioning

confidence: 99%

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GPCR-mediated β-arrestin activation deconvoluted with single-molecule precision

Asher

Terry

Gregorio

et al. 2022

Cell

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

GPCR-mediated β-arrestin activation deconvoluted with single-molecule precision

Asher

Terry

Gregorio

et al. 2022

Cell

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“…To the best of our knowledge, this peptide is the smallest described effective molecular scaffold of the ASK1-MKK4/7-JNK3 cascade or any MAPK cascade. This peptide does not have most elements involved in binding GPCRs (reviewed in [ 22 , 39 ]), ERK2 and its upstream activators [ 34 , 40 ], Src family kinases [ 41 ], clathrin [ 3 ], clathrin adaptor AP2 [ 5 ], calmodulin [ 42 ], and other known arrestin partners. Our finding suggests that other relatively small arrestin elements might be largely responsible for individual scaffolding functions.…”

Section: Discussionmentioning

confidence: 99%

Short Arrestin-3-Derived Peptides Activate JNK3 in Cells

Perry-Hauser

Kaoud

Stoy

et al. 2022

IJMS

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Arrestins were first discovered as suppressors of G protein-mediated signaling by G protein-coupled receptors. It was later demonstrated that arrestins also initiate several signaling branches, including mitogen-activated protein kinase cascades. Arrestin-3-dependent activation of the JNK family can be recapitulated with peptide fragments, which are monofunctional elements distilled from this multi-functional arrestin protein. Here, we use maltose-binding protein fusions of arrestin-3-derived peptides to identify arrestin elements that bind kinases of the ASK1-MKK4/7-JNK3 cascade and the shortest peptide facilitating JNK signaling. We identified a 16-residue arrestin-3-derived peptide expressed as a Venus fusion that leads to activation of JNK3α2 in cells. The strength of the binding to the kinases does not correlate with peptide activity. The ASK1-MKK4/7-JNK3 cascade has been implicated in neuronal apoptosis. While inhibitors of MAP kinases exist, short peptides are the first small molecule tools that can activate MAP kinases.

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“…Arrestin-3 also has higher affinity for clathrin [74]. The two non-visual subtypes appear to bind ERK2 differently [75]. Most strikingly, arrestin-3 facilitates the activation of JNK family kinases, whereas arrestin-2 does not [76][77][78].…”

Section: Arrestin-3mentioning

confidence: 98%

Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins

Gurevich

2022

IJMS

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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.

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The Two Non-Visual Arrestins Engage ERK2 Differently

Cited by 15 publications

References 84 publications

GPCR-mediated β-arrestin activation deconvoluted with single-molecule precision

GPCR-mediated β-arrestin activation deconvoluted with single-molecule precision

Short Arrestin-3-Derived Peptides Activate JNK3 in Cells

Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins

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