Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding
نویسندگان
چکیده
منابع مشابه
Active site-directed inactivation of constitutively active mutants of rhodopsin.
Recently, mutations of the active site Lys296 residue in rhodopsin (Lys296-->Glu and Lys296-->Met) have been found as the cause of disease in some patients with autosomal dominant retinitis pigmentosa. In vitro, these mutations result in constitutive activation of the protein. In an effort to develop a potential therapeutic agent for treatment of the disease, we have examined various amine deri...
متن کاملArrestin residues involved in the functional binding of arrestin to phosphorylated, photolyzed rhodopsin.
PURPOSE The purpose of our study was to determine whether arrestin residues previously predicted by computational modeling to interact with an aspartic acid substituted rhodopsin tail are actually involved in interactions with phospho-residues on the rhodopsin cytoplasmic tail. METHODS We generated arrestin mutants with altered charges at predicted positions. These mutants were then tested fo...
متن کاملDeactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants.
Arrestins constitute a family of small cytoplasmic proteins that mediate deactivation of G-protein-coupled receptors (GPCRs) and are known to be essential for cascade inactivation and receptor desensitization. Alternative splicing produces an array of arrestin gene products that have widely different specificities for their cognate receptors in vitro, but the differential functions of these spl...
متن کاملPhosphorylated rhodopsin and heparin induce similar conformational changes in arrestin.
Photoactivated rhodopsin is quenched upon its phosphorylation in the reaction catalyzed by rhodopsin kinase and the subsequent binding of a regulatory protein, arrestin. We have found that heparin and other polyanions compete with photoactivated, phosphorylated rhodopsin to bind arrestin (48-kDa protein, S-antigen). This is shown (a) by the suppression of stabilized metarhodopsin II; (b) by cha...
متن کاملDynamics 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...
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ژورنال
عنوان ژورنال: Cellular Signalling
سال: 2013
ISSN: 0898-6568
DOI: 10.1016/j.cellsig.2013.07.009