Rhodopsin Phosphorylation Sites and Their Role in Arrestin Binding
نویسندگان
چکیده
منابع مشابه
Dynamics of arrestin-rhodopsin interactions: acidic phospholipids enable binding of arrestin to purified rhodopsin in detergent.
We report that acidic phospholipids can restore the binding of visual arrestin to purified rhodopsin solubilized in n-dodecyl-beta-d-maltopyranoside. We used this finding to investigate the interplay between arrestin binding and the status of the retinal chromophore ligand in the receptor binding pocket. Our results showed that arrestin can interact with the late photoproduct Meta III and conve...
متن کاملRole of rhodopsin and arrestin phosphorylation in retinal degeneration of Drosophila.
Arrestins belong to a family of multifunctional adaptor proteins that regulate internalization of diverse receptors including G-protein-coupled receptors (GPCRs). Defects associated with endocytosis of GPCRs have been linked to human diseases. We used enhanced green fluorescent protein-tagged arrestin 2 (Arr2) to monitor the turnover of the major rhodopsin (Rh1) in live Drosophila. We demonstra...
متن کاملRhodopsin TM6 Can Interact with Two Separate and Distinct Sites on Arrestin: Evidence for Structural Plasticity and Multiple Docking Modes in Arrestin–Rhodopsin Binding
Various studies have implicated the concave surface of arrestin in the binding of the cytosolic surface of rhodopsin. However, specific sites of contact between the two proteins have not previously been defined in detail. Here, we report that arrestin shares part of the same binding site on rhodopsin as does the transducin Gα subunit C-terminal tail, suggesting binding of both proteins to rhodo...
متن کاملEnhanced Arrestin Facilitates Recovery and Protects Rods Lacking Rhodopsin Phosphorylation
G protein-coupled receptors (GPCRs) are the largest family of signaling proteins expressed in every cell in the body and are targeted by the majority of clinically used drugs [1]. GPCR signaling, including rhodopsin-driven phototransduction, is terminated by receptor phosphorylation followed by arrestin binding [2]. Genetic defects in receptor phosphorylation and excessive signaling by overacti...
متن کاملDistinct phosphorylation sites in the SST2A somatostatin receptor control internalization, desensitization, and arrestin binding.
The somatostatin subtype 2A (sst2A) receptor, a member of the G protein-coupled receptor superfamily, mediates many of the neuroendocrine and neuromodulatory actions of somatostatin, and it represents the primary target for somatostatin analogs used in cancer therapy and tumor localization. Agonist stimulation leads to the rapid phosphorylation, endocytosis, and desensitization of the sst2A rec...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1997
ISSN: 0021-9258
DOI: 10.1074/jbc.272.23.14762