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Trafficking of preassembled opioid mu-delta heterooligomer-Gz signaling complexes to the plasma membrane: coregulation by agonists.

Abstract：

:The cellular site of formation, Galpha-coupling preference, and agonist regulation of mu-delta opioid receptor (OR) heterooligomers were studied. Bioluminescence resonance energy transfer (BRET) showed that mu-deltaOR heterooligomers, composed of preformed mu and delta homooligomers, interacted constitutively in the endoplasmic reticulum (ER) with Galpha-proteins forming heteromeric signaling complexes before being targeted to the plasma membrane. Compared to muOR homooligomers, the mu-delta heterooligomers showed higher affinity and efficiency of interaction for Gz over Gi, indicating a switch in G-protein preference. Treatment with DAMGO or deltorphin II led to coregulated internalization of both receptors, whereas DPDPE and DSLET had no effect on mu-delta internalization. Staggered expression resulted in non-interacting mu and delta receptors, even though both receptors were colocalized at the cell surface. Agonists failed to induce BRET between staggered receptors, and resulted in internalization solely of the receptor targeted by agonist. Thus, mu-deltaOR heterooligomers form and preferentially associate with Gz to generate a signaling complex in the ER, and have a distinct agonist-internalization profile compared to either mu or delta homooligomers.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Hasbi A,Nguyen T,Fan T,Cheng R,Rashid A,Alijaniaram M,Rasenick MM,O'Dowd BF,George SR

doi

10.1021/bi701436w

subject

Has Abstract

pub_date

2007-11-13 00:00:00

pages

12997-3009

issue

45

eissn

0006-2960

issn

1520-4995

journal_volume

46

pub_type

杂志文章

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