Differential palmitoylation of two mouse glutamate receptor interacting protein 1 forms with different N-terminal sequences

2001 ◽  
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Maya Yamazaki ◽  
Masahiro Fukaya ◽  
Manabu Abe ◽  
Kanju Ikeno ◽  
Toshikazu Kakizaki ◽  
...  
2013 ◽  
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Pavel I Ortinski ◽  
Richard L Huganir ◽  
R Christopher Pierce

2008 ◽  
Vol 105 (6) ◽  
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Wendou Yu ◽  
Erik I. Charych ◽  
David R. Serwanski ◽  
Rong-wen Li ◽  
Rashid Ali ◽  
...  

2002 ◽  
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Jing-Song Fan ◽  
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Ya-Wei Shi ◽  
Mingjie Zhang

2019 ◽  
Vol 157 ◽  
pp. 107672 ◽  
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Andre U. Deutschmann ◽  
Anna G. McGrath ◽  
Vinay Parikh ◽  
Lisa A. Briand

2020 ◽  
Vol 6 (33) ◽  
pp. eabb9110
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...  

The biophysical and molecular mechanisms that enable animals to detect magnetic fields are unknown. It has been proposed that birds have a light-dependent magnetic compass that relies on the formation of radical pairs within cryptochrome molecules. Using spectroscopic methods, we show that pigeon cryptochrome clCRY4 is photoreduced efficiently and forms long-lived spin-correlated radical pairs via a tetrad of tryptophan residues. We report that clCRY4 is broadly and stably expressed within the retina but enriched at synapses in the outer plexiform layer in a repetitive manner. A proteomic survey for retinal-specific clCRY4 interactors identified molecules that are involved in receptor signaling, including glutamate receptor–interacting protein 2, which colocalizes with clCRY4. Our data support a model whereby clCRY4 acts as an ultraviolet-blue photoreceptor and/or a light-dependent magnetosensor by modulating glutamatergic synapses between horizontal cells and cones.


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