PMID- 18378118
OWN - NLM
STAT- MEDLINE
DCOM- 20080929
LR  - 20211020
IS  - 0898-6568 (Print)
IS  - 0898-6568 (Linking)
VI  - 20
IP  - 6
DP  - 2008 Jun
TI  - Endoplasmic reticulum export of adrenergic and angiotensin II receptors is 
      differentially regulated by Sar1 GTPase.
PG  - 1035-43
LID - 10.1016/j.cellsig.2008.01.014 [doi]
AB  - The molecular mechanism underlying the export of G protein-coupled receptors 
      (GPCRs) from the endoplasmic reticulum (ER) remains largely unknown. In this 
      manuscript, we investigated the role of Sar1 GTPase, which coordinates the 
      assembly and budding of COPII-coated vesicles, in the cell-surface targeting, 
      signaling and ER export of alpha(2B)-adrenergic (alpha(2B)-AR), beta(2)-AR and 
      angiotensin II type 1 receptors (AT1R). The cell-surface expression of 
      alpha(2B)-AR, beta(2)-AR and AT1R, and receptor-mediated ERK1/2 activation were 
      significantly attenuated by the GTP-bound mutant Sar1H79G, suggesting that export 
      from the ER of these receptors is mediated through the Sar1-dependent 
      COPII-coated vesicles. Interestingly, subcellular distribution analyses showed 
      that alpha(2B)-AR and AT1R were highly concentrated at discrete locations near 
      the nucleus in cells expressing Sar1H79G, whereas beta(2)-AR exhibited an ER 
      distribution. These data indicate that Sar1-catalyzed efficient GTP hydrolysis 
      differentially regulates ER export of adrenergic and angiotensin II receptors. 
      These data provide the first evidence indicating distinct mechanisms for the 
      recruitment of different GPCRs into the COPII vesicles on the ER membrane.
FAU - Dong, Chunmin
AU  - Dong C
AD  - Department of Pharmacology and Experimental Therapeutics, Louisiana State 
      University Health Sciences Center, 1901 Perdido St., New Orleans, LA 70112, 
      United States.
FAU - Zhou, Fuguo
AU  - Zhou F
FAU - Fugetta, Erin K
AU  - Fugetta EK
FAU - Filipeanu, Catalin M
AU  - Filipeanu CM
FAU - Wu, Guangyu
AU  - Wu G
LA  - eng
GR  - R01 GM076167/GM/NIGMS NIH HHS/United States
GR  - R01 GM076167-02/GM/NIGMS NIH HHS/United States
GR  - GM076167/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20080129
PL  - England
TA  - Cell Signal
JT  - Cellular signalling
JID - 8904683
RN  - 0 (ADRA2B protein, human)
RN  - 0 (Receptor, Angiotensin, Type 1)
RN  - 0 (Receptors, Adrenergic)
RN  - 0 (Receptors, Adrenergic, alpha-2)
RN  - 0 (Receptors, Adrenergic, beta-2)
RN  - EC 3.6.1.- (SAR1A protein, human)
RN  - EC 3.6.5.2 (Monomeric GTP-Binding Proteins)
SB  - IM
MH  - Cell Line
MH  - Cell Membrane/metabolism
MH  - Endoplasmic Reticulum/chemistry/*enzymology/metabolism
MH  - Humans
MH  - Monomeric GTP-Binding Proteins/genetics/*metabolism
MH  - Mutation
MH  - Protein Transport
MH  - Receptor, Angiotensin, Type 1/analysis/*metabolism
MH  - Receptors, Adrenergic/*metabolism
MH  - Receptors, Adrenergic, alpha-2/analysis/metabolism
MH  - Receptors, Adrenergic, beta-2/analysis/metabolism
MH  - Signal Transduction
PMC - PMC2413292
MID - NIHMS50557
EDAT- 2008/04/02 09:00
MHDA- 2008/09/30 09:00
PMCR- 2009/06/01
CRDT- 2008/04/02 09:00
PHST- 2007/11/10 00:00 [received]
PHST- 2008/01/03 00:00 [revised]
PHST- 2008/01/04 00:00 [accepted]
PHST- 2008/04/02 09:00 [pubmed]
PHST- 2008/09/30 09:00 [medline]
PHST- 2008/04/02 09:00 [entrez]
PHST- 2009/06/01 00:00 [pmc-release]
AID - S0898-6568(08)00011-9 [pii]
AID - 10.1016/j.cellsig.2008.01.014 [doi]
PST - ppublish
SO  - Cell Signal. 2008 Jun;20(6):1035-43. doi: 10.1016/j.cellsig.2008.01.014. Epub 
      2008 Jan 29.