Journal article
The association of arrestin-3 with the follitropin receptor depends on receptor activation and phosphorylation
Molecular and cellular endocrinology, Vol.204(1-2), pp.127-140
06/30/2003
DOI: 10.1016/S0303-7207(03)00088-1
PMID: 12850288
Abstract
We have recently shown that the binding of arrestin-3 to the lutropin receptor (LHR) is dependent mostly on receptor activation rather than on phosphorylation. The experiments presented here were designed to test the involvement of these two events in the association of arrestin-3 with the closely related follitropin receptor (FSHR). Activation of the FSHR leads to the phosphorylation of residues in the first and third intracellular loops. Mutation of the phosphorylation sites in the third intracellular loop of the rat (r) FSHR partially reduces phosphorylation but has no effect on arrestin-3 association. Mutation of the phosphorylation sites in the first intracellular loop abolishes phosphorylation and arrestin-3 association. Dominant-negative mutants of G protein-coupled receptor kinase (GRKs) 2 and 6 inhibit rFSHR phosphorylation to the same extent but only the dominant-negative mutant of GRK2 inhibits arrestin-3 association. Two mutations of the rFSHR (D389N and Y530F) that impair activation and abolish phosphorylation also impair arrestin-3 binding. GRK2 restores the phosphorylation of both mutants but it restores arrestin-3 association only to the D389N mutant. We conclude that, in contrast to the data obtained with the LHR, the association of arrestin-3 with the FSHR is dependent on receptor phosphorylation. The phosphorylation of the third intracellular loop residues is not needed for arrestin-3 association, however. © 2003 Elsevier Science Ireland Ltd. All rights reserved.
Details
- Title: Subtitle
- The association of arrestin-3 with the follitropin receptor depends on receptor activation and phosphorylation
- Creators
- Hanumanthappa Krishnamurthy - University of IowaColette Galet - University of IowaMario Ascoli - University of Iowa
- Resource Type
- Journal article
- Publication Details
- Molecular and cellular endocrinology, Vol.204(1-2), pp.127-140
- DOI
- 10.1016/S0303-7207(03)00088-1
- PMID
- 12850288
- NLM abbreviation
- Mol Cell Endocrinol
- ISSN
- 0303-7207
- eISSN
- 1872-8057
- Number of pages
- 14
- Grant note
- R01HD028962 / Eunice Kennedy Shriver National Institute of Child Health and Human Development (http://data.elsevier.com/vocabulary/SciValFunders/100009633) DK-25295 / National Institutes of Health (http://data.elsevier.com/vocabulary/SciValFunders/100000002) National Institutes of Health (http://data.elsevier.com/vocabulary/SciValFunders/100000002) Eunice Kennedy Shriver National Institute of Child Health and Human Development (http://data.elsevier.com/vocabulary/SciValFunders/100009633) Diabetes and Endocrinology Research Center of the University of Iowa
- Language
- English
- Date published
- 06/30/2003
- Academic Unit
- Injury Prevention Research Center; Neuroscience and Pharmacology; University of Iowa Health Care
- Record Identifier
- 9985137928602771
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