2005
DOI: 10.1074/jbc.m411341200
|View full text |Cite
|
Sign up to set email alerts
|

Dynamics of Arrestin-Rhodopsin Interactions

Abstract: In this study, we address the mechanism of visual arrestin release from light-activated rhodopsin using fluorescently labeled arrestin mutants. We find that two mutants, I72C and S251C, when labeled with the small, solvent-sensitive fluorophore monobromobimane, exhibit spectral changes only upon binding light-activated, phosphorylated rhodopsin. Our analysis indicates that these changes are probably due to a burying of the probes at these sites in the rhodopsin-arrestin or phospholipid-arrestin interface. Usin… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

5
57
1

Year Published

2006
2006
2018
2018

Publication Types

Select...
7
2

Relationship

2
7

Authors

Journals

citations
Cited by 69 publications
(63 citation statements)
references
References 66 publications
5
57
1
Order By: Relevance
“…5A, inset). This effect is similar to that previously reported for bimane-labeled arrestin (40). ArrestinRho*P binding stoichiometry was determined by titrating IANBD-labeled arrestin against a fixed amount of receptor and measuring the fluorescence intensity before and after photoactivation (Fig.…”
Section: Resultssupporting
confidence: 80%
See 1 more Smart Citation
“…5A, inset). This effect is similar to that previously reported for bimane-labeled arrestin (40). ArrestinRho*P binding stoichiometry was determined by titrating IANBD-labeled arrestin against a fixed amount of receptor and measuring the fluorescence intensity before and after photoactivation (Fig.…”
Section: Resultssupporting
confidence: 80%
“…In addition, some portion of our ROS-P preparations may have been non-or under-phosphorylated. 5 Our phosphorylation procedure, based on one previously established, yielded an average of ϳ6 phosphates per rhodopsin (40). Although we did not directly analyze the different phosphorylated species present in our ROS-P samples, a previous report (44) suggests that up to 10% of the rhodopsin in our samples may have had less than the required two phosphates necessary for arrestin activation and binding (45).…”
Section: Resultsmentioning
confidence: 93%
“…The interaction of arrestin occurs Binding promiscuity of the arrestin-1 finger loop via initial "pre-binding" to the phosphorylated receptor (5) followed by binding of the arrestin "finger loop" (6,7) which recognizes the active receptor conformation (8). The necessity of pre-binding is circumvented in the naturally occurring arrestin splice variant p44 lacking the C-tail (9,10).…”
mentioning
confidence: 99%
“…Preparation of Rod Outer Segments and Purification of Rho-ROS and highly phosphorylated ROS were prepared from bovine retinas as described previously (5).…”
mentioning
confidence: 99%