Structural Mechanism of the Arrestin-3/JNK3 Interaction
نویسندگان
چکیده
منابع مشابه
Modulation of the arrestin-clathrin interaction in cells. Characterization of beta-arrestin dominant-negative mutants.
We recently demonstrated that nonvisual arrestins interact via a C-terminal binding domain with clathrin and function as adaptor proteins to promote beta2-adrenergic receptor (beta2AR) internalization. Here, we investigated the potential utility of a mini-gene expressing the clathrin-binding domain of beta-arrestin (beta-arrestin (319-418)) to function as a dominant-negative with respect to bet...
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PURPOSE Arrestin is in disequilibrium in photoreceptors, translocating between inner and outer segments in response to light. The purpose of this project was to identify the cellular component with which arrestin associates in the dark-adapted retina. METHODS Retinas were cross-linked with 2.5 mM dithiobis(succinimidylpropionate) (DSP), and arrestin-containing complexes purified by anion-exch...
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The interaction between nano-SiO2 and lysozyme was investigated by the method of UV-Visible detection and fluorescence spectroscopic techniques. The thermal denaturation of lysozyme has been investigated in the presence and absence of nano-SiO2 over the temperature range (293-373) K in different buffers and pH values, using temperature scanning spectroscopy. The presence of nano-SiO2 caused th...
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Recent studies have revealed that light adaptation of both vertebrate and invertebrate photoreceptors is accompanied by massive translocations of major signaling proteins in and out of the cellular compartments where visual signal transduction takes place. In this issue of Neuron, Lee and Montell report a breakthrough in understanding the mechanism of arrestin translocation in Drosophila. They ...
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ژورنال
عنوان ژورنال: Structure
سال: 2019
ISSN: 0969-2126
DOI: 10.1016/j.str.2019.04.002