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Papers In Press, published online ahead of print November 5, 2001
Department of Pharmacology, The University of Iowa, Iowa city, IA 52242-1109
Corresponding Author: mario-ascoli{at}uiowa.edu
Although the involvement of the non-visual arrestins in the agonist-induced internalization of the hLHR has been previously documented with the use of dominant-negative mutants, a physical association of the non-visual arrestins with the hLHR in intact cells has not been established. In the studies presented herein we used a crosslinking/coimmunoprecipitation/immunoblotting approach as well as confocal microscopy to document the association of the hLHR with the non-visual 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/non-visual 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 GPCRS (i.e., the b2adrenergic receptor, the m2 muscarinic receptor, rhodopsin, and the type1A angiotensin receptor) where arrestin binding depends mostly on receptor phosphorylation rather than on receptor activation. We have also examined the association of the non-visual 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 non-visual arrestins in an agonist-independent fashion.
J. Biol. Chem, 10.1074/jbc.M106082200
Submitted on June 29, 2001
Revised on October 22, 2001
Accepted on November 5, 2001
The association of arrestin-3 with the human lutropin/choriogonadotropin receptor depends mostly on receptor activation rather than on receptor phosphorylation
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