gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Component of oligomeric golgi complex 7

The protein encoded by this gene resides in the golgi, and constitutes one of the 8 subunits of the conserved oligomeric Golgi (COG) complex, which is required for normal golgi morphology and localization. Mutations in this gene are associated with the congenital disorder of glycosylation type IIe.[provided by RefSeq, May 2010] (from NCBI)
Top mentioned proteins: COG4, Transferrin, CAN, COD2, ACID
Papers on COG7
Cog5-Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex.
Hughson et al., Tomsk, Russia. In Proc Natl Acad Sci U S A, 2014
Here, we report the crystal structure of a complex between two lobe B subunits, Cog5 and Cog7.
Target silencing of components of the conserved oligomeric Golgi complex impairs HIV-1 replication.
Dykxhoorn et al., Miami, United States. In Virus Res, 2014
The targeted silencing of components of lobe B of the COG complex, namely COG5, COG6, COG7 and COG8, inhibited HIV-1 replication.
Congenital disorders of glycosylation with emphasis on cerebellar involvement.
Jaeken et al., Catania, Italy. In Semin Neurol, 2014
It has also been reported in some patients with ALG1-CDG, ALG3-CDG, ALG9-CDG, ALG6-CDG, ALG8-CDG, PIGA-CDG, DPM1-CDG, DPM2-CDG, B4GALT1-CDG, SLC35A2-CDG, COG1-CDG, COG5-CDG, COG7-CDG, and COG8-CDG.
Multipronged interaction of the COG complex with intracellular membranes.
Lupashin et al., Little Rock, United States. In Cell Logist, 2014
Moreover, COG subunits remained membrane-associated even in COG4 and COG7 depleted cells when Golgi architecture was severely affected.
Wrinkled skin and fat pads in patients with ALG8-CDG: revisiting skin manifestations in congenital disorders of glycosylation.
Morava et al., In Pediatr Dermatol, 2014
Some of these conditions, including PMM2-CDG, frequently present with recognizable skin abnormalities such as abnormal fat distribution, skin wrinkling, or peau d'orange, whereas others, such as COG7-CDG and ATP6V0A2-CDG, have been described in association with cutis laxa: wrinkled, inelastic, and sagging skin.
Deficiency of the Cog8 subunit in normal and CDG-derived cells impairs the assembly of the COG and Golgi SNARE complexes.
Lev et al., Israel. In Traffic, 2013
The assembly of these SNARE complexes is also impaired in cells derived from a Cog7-deficient CDG patient.
Pathway analysis of a genome-wide association study in schizophrenia.
Song et al., Seoul, South Korea. In Gene, 2013
However, 13 of candidate genes (RDH8, ACVR1, PSMD9, KCNAB1, SLC17A3, ARCN1, COG7, STAB2, LRPAP1, STAB1, CXCL16, COL4A4, EXOSC3) and 9 of candidate pathways were novel.
Mutations in Cog7 affect Golgi structure, meiotic cytokinesis and sperm development during Drosophila spermatogenesis.
Giansanti et al., Roma, Italy. In J Cell Sci, 2012
Deletions in the human COG7 gene are associated with a rare multisystemic congenital disorder of glycosylation that causes mortality within the first year of life.
COG5-CDG: expanding the clinical spectrum.
Jaeken et al., Leuven, Belgium. In Orphanet J Rare Dis, 2011
Interestingly, on a clinical basis some of the patients present a significant overlap with COG7-CDG, a finding which can probably be explained by subunit interactions at the protein level.
Metabolic cutis laxa syndromes.
Morava et al., Nijmegen, Netherlands. In J Inherit Metab Dis, 2011
The discovery of the COG7 defect in patients with wrinkled, inelastic skin was the first genetic link with the Congenital Disorders of Glycosylation (CDG).
Plasma N-glycan profiling by mass spectrometry for congenital disorders of glycosylation type II.
Lefeber et al., Nijmegen, Netherlands. In Clin Chem, 2011
CDGs due to defects in proteins involved in Golgi trafficking, such as subunit 7 of the conserved oligomeric Golgi complex (COG7) and subunit V0 a2 of the lysosomal H(+)-transporting ATPase (ATP6V0A2) caused a loss of triantennary N-glycans and an increase of truncated structures.
Interaction of Golgin-84 with the COG complex mediates the intra-Golgi retrograde transport.
Oda et al., Niigata, Japan. In Traffic, 2010
Protein interaction analyses have revealed that golgin-84 interacts with another tether, the conserved oligomeric Golgi (COG) complex, through its subunit Cog7.
Deficiency in COG5 causes a moderate form of congenital disorders of glycosylation.
Hennet et al., Z├╝rich, Switzerland. In Hum Mol Genet, 2009
To date, mutations in COG1, COG4, COG7 and COG8 genes have been associated with diseases, which range from severe multi-organ disorders to moderate forms of neurological impairment.
A new mutation in COG7 extends the spectrum of COG subunit deficiencies.
Jaeken et al., Leuven, Belgium. In Eur J Med Genet, 2009
A new mutation in COG7 extends the spectrum of COG subunit deficiencies.
Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation.
Lupashin et al., Little Rock, United States. In Carbohydr Res, 2008
A deletion of Lobe A COG subunits in yeasts causes severe growth defects while mutations in COG1, COG7, and COG8 in humans cause novel types of congenital disorders of glycosylation.
A common mutation in the COG7 gene with a consistent phenotype including microcephaly, adducted thumbs, growth retardation, VSD and episodes of hyperthermia.
Wevers et al., Nijmegen, Netherlands. In Eur J Hum Genet, 2007
A homozygous, intronic splice site mutation (c.169+4A>C) of the COG7 gene was identified in 3 patients with Congenital Disorder of Glycosylation type IIe.
COG-7-deficient Human Fibroblasts Exhibit Altered Recycling of Golgi Proteins.
Kornfeld et al., Saint Louis, United States. In Mol Biol Cell, 2006
Retrograde transport of multiple Golgi proteins to the ER in COG-7-deficient patient fibroblasts via brefeldin A-induced tubules was significantly slower than occurs in normal fibroblasts.
Genetic analysis of the subunit organization and function of the conserved oligomeric golgi (COG) complex: studies of COG5- and COG7-deficient mammalian cells.
Krieger et al., Cambridge, United States. In J Biol Chem, 2005
COG5- and COG7 subunits play distinctive roles in controlling Golgi structure and function
Mutation of the COG complex subunit gene COG7 causes a lethal congenital disorder.
Freeze et al., Los Angeles, United States. In Nat Med, 2004
Here we describe two siblings with a fatal form of CDG caused by a mutation in the gene encoding COG-7, a subunit of the conserved oligomeric Golgi (COG) complex.
share on facebooktweetadd +1mail to friends