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 convert it to a Meta II-like species. Interestingly in these mixed micelles, the release of retinal and arrestin was no longer directly coupled as it is in the native rod disk membrane. For example, up to approximately 50% of the retinal could be released even though arrestin remains bound to the receptor in a long lived complex. We anticipate that this new ability to study these proteins in a defined, purified system will facilitate further structural and dynamic studies of arrestin-rhodopsin interactions.
Sommer
Martha E
ME
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239-3098, USA.
Smith
W Clay
WC
Farrens
David L
DL
D000818:Animals; D019393:Arrestin / Q000378:metabolism*; D002417:Cattle; D008024:Ligands; D008320:Maltose / Q000031:analogs & derivatives / Q000378:metabolism; D008823:Micelles; D010743:Phospholipids / Q000502:physiology*; D011485:Protein Binding; D012160:Retina / Q000502:physiology; D012172:Retinaldehyde / Q000378:metabolism; D012243:Rhodopsin / Q000378:metabolism*; D012995:Solubility
D019393:Arrestin; D008024:Ligands; D008823:Micelles; D010743:Phospholipids; C411362:dodecyl maltopyranoside; D008320:Maltose; D012243:Rhodopsin; D012172:Retinaldehyde