In:
Science, American Association for the Advancement of Science (AAAS), Vol. 315, No. 5812 ( 2007-02-02), p. 663-666
Abstract:
Seven-transmembrane receptor (7TMR) signaling is transduced by second messengers such as diacylglycerol (DAG) generated in response to the heterotrimeric guanine nucleotide–binding protein G q and is terminated by receptor desensitization and degradation of the second messengers. We show that β-arrestins coordinate both processes for the G q -coupled M1 muscarinic receptor. β-Arrestins physically interact with diacylglycerol kinases (DGKs), enzymes that degrade DAG. Moreover, β-arrestins are essential for conversion of DAG to phosphatidic acid after agonist stimulation, and this activity requires recruitment of the β-arrestin–DGK complex to activated 7TMRs. The dual function of β-arrestins, limiting production of diacylglycerol (by receptor desensitization) while enhancing its rate of degradation, is analogous to their ability to recruit adenosine 3′,5′-monophosphate phosphodiesterases to G s -coupled β 2 -adrenergic receptors. Thus, β-arrestins can serve similar regulatory functions for disparate classes of 7TMRs through structurally dissimilar enzymes that degrade chemically distinct second messengers.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.1134562
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2007
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
