PMID- 15728195
OWN - NLM
STAT- MEDLINE
DCOM- 20050418
LR  - 20181113
IS  - 0021-9525 (Print)
IS  - 1540-8140 (Electronic)
IS  - 0021-9525 (Linking)
VI  - 168
IP  - 5
DP  - 2005 Feb 28
TI  - Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa 
      cells.
PG  - 747-59
AB  - The conserved oligomeric Golgi (COG) complex is an evolutionarily conserved 
      multi-subunit protein complex that regulates membrane trafficking in eukaryotic 
      cells. In this work we used short interfering RNA strategy to achieve an 
      efficient knockdown (KD) of Cog3p in HeLa cells. For the first time, we have 
      demonstrated that Cog3p depletion is accompanied by reduction in Cog1, 2, and 4 
      protein levels and by accumulation of COG complex-dependent (CCD) vesicles 
      carrying v-SNAREs GS15 and GS28 and cis-Golgi glycoprotein GPP130. Some of these 
      CCD vesicles appeared to be vesicular coat complex I (COPI) coated. A prolonged 
      block in CCD vesicles tethering is accompanied by extensive fragmentation of the 
      Golgi ribbon. Fragmented Golgi membranes maintained their juxtanuclear 
      localization, cisternal organization and are competent for the anterograde 
      trafficking of vesicular stomatitis virus G protein to the plasma membrane. In a 
      contrast, Cog3p KD resulted in inhibition of retrograde trafficking of the Shiga 
      toxin. Furthermore, the mammalian COG complex physically interacts with GS28 and 
      COPI and specifically binds to isolated CCD vesicles.
FAU - Zolov, Sergey N
AU  - Zolov SN
AD  - Department of Physiology and Biophysics, University of Arkansas for Medical 
      Sciences, Little Rock, AR 72205, USA.
FAU - Lupashin, Vladimir V
AU  - Lupashin VV
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20050222
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (COG3 protein, S cerevisiae)
RN  - 0 (COG3 protein, human)
RN  - 0 (Coat Protein Complex I)
RN  - 0 (GOLIM4 protein, human)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (SNARE Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Vesicular Transport Proteins)
RN  - 75757-64-1 (Shiga Toxin)
SB  - IM
MH  - Adaptor Proteins, Vesicular Transport/*deficiency/metabolism
MH  - Animals
MH  - Coat Protein Complex I/metabolism
MH  - Cytoplasmic Vesicles/*metabolism/ultrastructure
MH  - Endoplasmic Reticulum/ultrastructure
MH  - Golgi Apparatus/*metabolism/ultrastructure
MH  - HeLa Cells
MH  - Humans
MH  - Membrane Glycoproteins/metabolism
MH  - Mice
MH  - Microscopy, Electron
MH  - Phosphoproteins/metabolism
MH  - Protein Transport/physiology
MH  - SNARE Proteins
MH  - Saccharomyces cerevisiae Proteins
MH  - Shiga Toxin/metabolism
MH  - Vesicular Transport Proteins/metabolism
PMC - PMC2171815
EDAT- 2005/02/25 09:00
MHDA- 2005/04/19 09:00
PMCR- 2005/08/28
CRDT- 2005/02/25 09:00
PHST- 2005/02/25 09:00 [pubmed]
PHST- 2005/04/19 09:00 [medline]
PHST- 2005/02/25 09:00 [entrez]
PHST- 2005/08/28 00:00 [pmc-release]
AID - jcb.200412003 [pii]
AID - 200412003 [pii]
AID - 10.1083/jcb.200412003 [doi]
PST - ppublish
SO  - J Cell Biol. 2005 Feb 28;168(5):747-59. doi: 10.1083/jcb.200412003. Epub 2005 Feb 
      22.