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FEBS Lett. 2010 Jun 3;584(11):2207-12. doi: 10.1016/j.febslet.2010.03.039. Epub 2010 Mar 29.

Beta-2 adrenergic receptor mediated ERK activation is regulated by interaction with MAGI-3.

Author information

1
Department of Biochemistry and Molecular Biology, Capital Medical University, Beijing, PR China.

Abstract

The beta-2 adrenergic receptor (beta2AR) has a carboxyl terminus motif that can interact with PSD-95/discs-large/ZO1 homology (PDZ) domain-containing proteins. In this paper, we identified membrane-associated guanylate kinase inverted-3 (MAGI-3) as a novel binding partner of beta2AR. The carboxyl terminus of beta2AR binds with high affinity to the fifth PDZ domain of MAGI-3, with the last four amino acids (D-S-L-L) of the receptor being the key determinants of the interaction. In cells, the association of full-length beta2AR with MAGI-3 occurs constitutively and is enhanced by agonist stimulation of the receptor. Our data also demonstrated that beta2AR-stimulated extracellular signal-regulated kinase-1/2 (ERK1/2) activation was substantially retarded by MAGI-3 expression. These data suggest that MAGI-3 regulates beta2AR-mediated ERK activation through the physical interaction between beta2AR and MAGI-3.

PMID:
20353789
DOI:
10.1016/j.febslet.2010.03.039
[Indexed for MEDLINE]
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