Journal article
The association of arrestin-3 with the human lutropin/choriogonadotropin receptor depends mostly on receptor activation rather than on receptor phosphorylation
The Journal of biological chemistry, Vol.277(1), pp.702-710
01/04/2002
DOI: 10.1074/jbc.M106082200
PMID: 11696538
Abstract
Although the involvement of the nonvisual arrestins in the agonist-induced internalization of the human lutropin receptor (hLHR) has been documented previously with the use of dominant-negative mutants, a physical association of the nonvisual arrestins with the hLHR in intact cells has not been established. In the studies presented herein, we used a cross-linking/coimmunoprecipitation/immunoblotting approach as well as confocal microscopy to document the association of the hLHR with the nonvisual arrestins in co-transfected 293 cells. We also used this approach to examine the relative importance of receptor activation and receptor phosphorylation in the formation of this complex. Using hLHR mutants that impair phosphorylation, activation, or both, we show that the formation of the hLHR-nonvisual arrestin complex depends mostly on the agonist-induced activation of the hLHR rather than on the phosphorylation of the hLHR. These results stand in contrast to those obtained with several other G protein-coupled receptors (i.e. the β2-adrenergic receptor, the m2 muscarinic receptor, rhodopsin, and the type 1A angiotensin receptor) where arrestin binding depends mostly on receptor phosphorylation rather than on receptor activation. We have also examined the association of the nonvisual arrestins with naturally occurring gain-of-function mutations of the hLHR found in boys with Leydig cell hyperplasia or Leydig cell adenomas. Our results show that these mutants associate with the nonvisual arrestins in an agonist-independent fashion.
Details
- Title: Subtitle
- The association of arrestin-3 with the human lutropin/choriogonadotropin receptor depends mostly on receptor activation rather than on receptor phosphorylation
- Creators
- Le Min - University of IowaColette Galet - University of IowaMario Ascoli - University of Iowa
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.277(1), pp.702-710
- DOI
- 10.1074/jbc.M106082200
- PMID
- 11696538
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Number of pages
- 9
- Grant note
- National Institute of Diabetes and Digestive and Kidney Diseases (http://data.elsevier.com/vocabulary/SciValFunders/100000062) P30DK025295 / National Institute of Diabetes and Digestive and Kidney Diseases (http://data.elsevier.com/vocabulary/SciValFunders/100000062)
- Language
- English
- Date published
- 01/04/2002
- Academic Unit
- Injury Prevention Research Center; Neuroscience and Pharmacology; University of Iowa Health Care
- Record Identifier
- 9985137927802771
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