PMID- 15178324
OWN - NLM
STAT- MEDLINE
DCOM- 20040722
LR  - 20191210
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 567
IP  - 2-3
DP  - 2004 Jun 4
TI  - Exocytic pathway-independent plasma membrane targeting of heterotrimeric G 
      proteins.
PG  - 209-13
AB  - Heterotrimeric G proteins are lipid-modified, peripheral membrane proteins that 
      function at the inner surface of the plasma membrane (PM) to relay signals from 
      cell-surface receptors to downstream effectors. Cellular trafficking pathways 
      that direct nascent G proteins to the PM are poorly defined. In this report, we 
      test the proposal that G proteins utilize the classical exocytic pathway for PM 
      targeting. PM localization of the G protein heterotrimers alpha s beta 1 gamma 2 
      and alpha q beta 1 gamma 2 occurred independently of treatment of cells with 
      Brefeldin A, which disrupts the Golgi, or expression of Sar1 mutants, which 
      prevent the formation of endoplasmic reticulum to Golgi transport vesicles. 
      Moreover, the palmitoylation of alpha q was unaffected by Brefeldin A treatment, 
      even though the palmitoylation of SNAP25 was blocked by Brefeldin A. 
      Non-palmitoylated mutants of alpha s and alpha q failed to stably bind to beta 
      gamma and displayed a dispersed cytoplasmic localization when co-expressed with 
      beta gamma. These findings support a refined model of the PM trafficking pathway 
      of G proteins, involving assembly of the heterotrimer at the endoplasmic 
      reticulum and transport to the PM independently of the Golgi.
FAU - Takida, Satoshi
AU  - Takida S
AD  - Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson 
      University, 233 S. 10th St., 839 BLSB, Philadelphia, PA 19107, USA.
FAU - Wedegaertner, Philip B
AU  - Wedegaertner PB
LA  - eng
PT  - Journal Article
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Biomarkers)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Palmitates)
RN  - 0 (Protein Subunits)
RN  - 0 (Recombinant Proteins)
RN  - 0 (SNAP25 protein, human)
RN  - 0 (Synaptosomal-Associated Protein 25)
RN  - 20350-15-6 (Brefeldin A)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.1 (Heterotrimeric GTP-Binding Proteins)
SB  - IM
MH  - Animals
MH  - Biomarkers
MH  - Brefeldin A/pharmacology
MH  - COS Cells
MH  - Cell Line
MH  - Cell Membrane/*metabolism
MH  - Chlorocebus aethiops
MH  - Exocytosis
MH  - GTP-Binding Proteins/genetics/metabolism
MH  - Golgi Apparatus/metabolism
MH  - Heterotrimeric GTP-Binding Proteins/chemistry/genetics/*metabolism
MH  - Humans
MH  - Membrane Proteins/genetics/metabolism
MH  - Nerve Tissue Proteins/metabolism
MH  - Palmitates/metabolism
MH  - Protein Subunits
MH  - Protein Transport
MH  - Recombinant Proteins/genetics/metabolism
MH  - Signal Transduction
MH  - Synaptosomal-Associated Protein 25
MH  - Transfection
EDAT- 2004/06/05 05:00
MHDA- 2004/07/23 05:00
CRDT- 2004/06/05 05:00
PHST- 2004/03/19 00:00 [received]
PHST- 2004/04/21 00:00 [revised]
PHST- 2004/04/22 00:00 [accepted]
PHST- 2004/06/05 05:00 [pubmed]
PHST- 2004/07/23 05:00 [medline]
PHST- 2004/06/05 05:00 [entrez]
AID - S0014579304005393 [pii]
AID - 10.1016/j.febslet.2004.04.062 [doi]
PST - ppublish
SO  - FEBS Lett. 2004 Jun 4;567(2-3):209-13. doi: 10.1016/j.febslet.2004.04.062.