PMID- 16420527
OWN - NLM
STAT- MEDLINE
DCOM- 20060327
LR  - 20141120
IS  - 1398-9219 (Print)
IS  - 1398-9219 (Linking)
VI  - 7
IP  - 2
DP  - 2006 Feb
TI  - COG complex-mediated recycling of Golgi glycosyltransferases is essential for 
      normal protein glycosylation.
PG  - 191-204
AB  - Defects in conserved oligomeric Golgi (COG) complex result in multiple 
      deficiencies in protein glycosylation. On the other hand, acute knock-down (KD) 
      of Cog3p (COG3 KD) causes accumulation of intra-Golgi COG complex-dependent (CCD) 
      vesicles. Here, we analyzed cellular phenotypes at different stages of COG3 KD to 
      uncover the molecular link between COG function and glycosylation disorders. For 
      the first time, we demonstrated that medial-Golgi enzymes are transiently 
      relocated into CCD vesicles in COG3 KD cells. As a result, Golgi modifications of 
      both plasma membrane (CD44) and lysosomal (Lamp2) glycoproteins are distorted. 
      Localization of these proteins is not altered, indicating that the COG complex is 
      not required for anterograde trafficking and accurate sorting. COG7 KD and double 
      COG3/COG7 KD caused similar defects with respect to both Golgi traffic and 
      glycosylation, suggesting that the entire COG complex orchestrates recycling of 
      medial-Golgi-resident proteins. COG complex-dependent docking of isolated CCD 
      vesicles was reconstituted in vitro, supporting their role as functional 
      trafficking intermediates. Altogether, the data suggest that constantly cycling 
      medial-Golgi enzymes are transported from distal compartments in CCD vesicles. 
      Dysfunction of COG complex leads to separation of glycosyltransferases from 
      anterograde cargo molecules passing along secretory pathway, thus affecting 
      normal protein glycosylation.
FAU - Shestakova, Anna
AU  - Shestakova A
AD  - Department of Physiology and Biophysics, University of Arkansas for Medical 
      Sciences, Little Rock, AR 72205, USA.
FAU - Zolov, Sergey
AU  - Zolov S
FAU - Lupashin, Vladimir
AU  - Lupashin V
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - England
TA  - Traffic
JT  - Traffic (Copenhagen, Denmark)
JID - 100939340
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (BET1L protein, human)
RN  - 0 (COG3 protein, human)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Qc-SNARE Proteins)
RN  - 0 (RNA, Small Interfering)
RN  - EC 2.4.- (Glycosyltransferases)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
RN  - EC 2.4.1.101 (alpha-1,3-mannosyl-glycoprotein 
      beta-1,2-N-acetylglucosaminyltransferase I)
SB  - IM
MH  - Adaptor Proteins, Vesicular Transport/antagonists & 
      inhibitors/genetics/*metabolism
MH  - Base Sequence
MH  - Glycosyltransferases/*metabolism
MH  - Golgi Apparatus/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - In Vitro Techniques
MH  - Membrane Glycoproteins/chemistry/metabolism
MH  - Models, Biological
MH  - Multiprotein Complexes
MH  - N-Acetylglucosaminyltransferases/metabolism
MH  - Phenotype
MH  - *Protein Processing, Post-Translational
MH  - Qc-SNARE Proteins/metabolism
MH  - RNA Interference
MH  - RNA, Small Interfering/genetics
EDAT- 2006/01/20 09:00
MHDA- 2006/03/28 09:00
CRDT- 2006/01/20 09:00
PHST- 2006/01/20 09:00 [pubmed]
PHST- 2006/03/28 09:00 [medline]
PHST- 2006/01/20 09:00 [entrez]
AID - TRA376 [pii]
AID - 10.1111/j.1600-0854.2005.00376.x [doi]
PST - ppublish
SO  - Traffic. 2006 Feb;7(2):191-204. doi: 10.1111/j.1600-0854.2005.00376.x.