Results 21 to 30 of about 871,508 (182)

A Brief History of the β-Arrestins [PDF]

Methods in Molecular Biology, 2019
Lawrence S Barak, Marc Caron
exaly   +2 more sources

Molecular evidence and clinical importance of β-arrestins expression in patients with acromegaly [PDF]

Journal of Cellular and Molecular Medicine, 2018
Leila Chimelli, Mari C. Vázquez-Borrego, Maria Caroline Alves Coelho   +2 more
exaly   +2 more sources

β-Arrestin regulation of myosin light chain phosphorylation promotes AT1aR-mediated cell contraction and migration. [PDF]

PLoS ONE, 2013
Over the last decade, it has been established that G-protein-coupled receptors (GPCRs) signal not only through canonical G-protein-mediated mechanisms, but also through the ubiquitous cellular scaffolds β-arrestin-1 and β-arrestin-2.
Elie Simard, Jeffrey J Kovacs, William E Miller, Jihee Kim, Michel Grandbois, Robert J Lefkowitz   +5 more
doaj   +1 more source

Differential Involvement of ACKR3 C-Tail in β-Arrestin Recruitment, Trafficking and Internalization

Cells, 2021
Background: The atypical chemokine receptor 3 (ACKR3) belongs to the superfamily of G protein-coupled receptors (GPCRs). Unlike classical GPCRs, this receptor does not activate G proteins in most cell types but recruits β-arrestins upon activation. ACKR3
Aurélien Zarca, Claudia Perez, Jelle van den Bor, Jan Paul Bebelman, Joyce Heuninck, Rianna J. F. de Jonker, Thierry Durroux, Henry F. Vischer, Marco Siderius, Martine J. Smit   +9 more
doaj   +1 more source

Select G-Protein-Coupled Receptors Modulate Agonist-Induced Signaling via a ROCK, LIMK, and β-Arrestin 1 Pathway

Cell Reports, 2013
G-protein-coupled receptors (GPCRs) are typically present in a basal, inactive state but, when bound to an agonist, activate downstream signaling cascades. In studying arrestin regulation of opioid receptors in dorsal root ganglia (DRG) neurons, we find that agonists of delta opioid receptors (δORs) activate cofilin through Rho-associated coiled-coil ...
Mittal, N, Roberts, K, Pal, K, Bentolila, LA, Fultz, E, Minasyan, A, Cahill, C, Pradhan, A, Conner, D, DeFea, K, Evans, C, Walwyn, W   +11 more
openaire   +6 more sources

An intrabody sensor to monitor conformational activation of β-arrestins

, 2022
Agonist-induced interaction of β-arrestins with GPCRs is critically involved in downstream signaling and regulation. This interaction is associated with activation and major conformational changes in β-arrestins.
Asuka Inoue, Sarma, Parishmita, Deeksha, S., Inoue, Asuka, S. Deeksha, Dwivedi-Agnihotri, Hemlata, Hemlata Dwivedi-Agnihotri, Parishmita Sarma, Kawakami, Kouki, Shukla, Arun K., Arun K. Shukla, Kouki Kawakami   +11 more
core   +1 more source

Expression of β-arrestins in toxic and cold thyroid nodules [PDF]

, 2000
β-Arrestins mediate agonist dependent desensitization of G protein-coupled receptors. Somatic TSH receptor mutations were identified in the majority of hot thyroid nodules.
Ralf Paschke, Holzapfel, Hans-Peter, Hans-Peter Holzapfel, Carsten Voigt, Voigt, Carsten, Paschke, Ralf   +5 more
core   +1 more source

Mammalian α arrestins link activated seven transmembrane receptors to Nedd4 family e3 ubiquitin ligases and interact with β arrestins. [PDF]

PLoS ONE, 2012
The complement of fungal cell surface proteins is widely regulated by ubiquitination of membrane proteins, which results in their endocytosis and vacuolar degradation.
Fortune F Shea, Jennie L Rowell, Yechaowei Li, Tien-Hsien Chang, Carlos E Alvarez   +4 more
doaj   +1 more source

Data_Sheet_1_ACKR4 Recruits GRK3 Prior to β-Arrestins but Can Scavenge Chemokines in the Absence of β-Arrestins.docx

, 2020
Chemokines are essential for guiding cell migration. Atypical chemokine receptors (ACKRs) contribute to the cell migration process by binding, internalizing and degrading local chemokines, which enables the formation of confined gradients.
Gianluca D'Agostino (5768691), Angela Salnikov (8745738), Marcus Thelen (164322), Ilona Kindinger (6202715), Christoph Matti (8745735), Marc Artinger (3234840), Mariagrazia Uguccioni (265126), Daniel F. Legler (8745741)   +7 more
core   +1 more source

Regulation of the Cardiac Potassium Channel Kir2.1 by the alpha-arrestins

, 2020
1. Kir2.1 is a mammalian potassium channel that is linked to numerous cardiac arrhythmias when it is unable to function or be trafficked correctly. 2.
Ceara K. McAtee (8729687), Allyson F. O'Donnell (201306), Jeffrey L Brodsky (55005), Marcel Bruchez (3882238), Adam V. Kwiatkowski (8729690), Natalie A. Hager (8729683)   +5 more
core   +1 more source