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COG4 Cog4p

COG4, SEC38, Cog4p
The protein encoded by this gene is a component of an oligomeric protein complex involved in the structure and function of the Golgi apparatus. Defects in this gene may be a cause of congenital disorder of glycosylation type IIj. Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Aug 2010] (from NCBI)
Top mentioned proteins: COG7, COD2, CAN, Syntaxin 16, c-Myc
Papers on COG4
Mutations in COG2 encoding a subunit of the conserved oligomeric golgi complex cause a congenital disorder of glycosylation.
Saitsu et al., Yokohama, Japan. In Clin Genet, May 2015
Protein expression of COG2, along with COG3 and COG4, was decreased in fibroblasts from the patient.
Mutations in proteins of the Conserved Oligomeric Golgi Complex affect polarity, cell wall structure, and glycosylation in the filamentous fungus Aspergillus nidulans.
Hill et al., Savannah, United States. In Fungal Genet Biol, 2014
were identified as homologues of COG2 and COG4, respectively, each predicted to encode a subunit of the multi-protein COG (Conserved Oligomeric Golgi) Complex involved in retrograde vesicle trafficking in the Golgi apparatus.
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
Despite some progress toward this goal, including EM studies of COG lobe A (subunits 1-4) and higher-resolution structures of portions of Cog2 and Cog4, the structures of COG's eight subunits and the principles governing their assembly are mostly unknown.
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.
Identified single-nucleotide polymorphisms and haplotypes at 16q22.1 increase diabetic nephropathy risk in Han Chinese population.
Tsai et al., In Bmc Genet, 2013
In haplotype association tests, identified haplotypes located in the chromosome 16q22.1 region (containing ST3GAL2, COG4, SF3B3, and IL34 genes) raised DN risk.
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
Likewise, the integrity of the COG complex is also impaired in Cog1-, Cog4- and Cog6-depleted cells.
COG complexes form spatial landmarks for distinct SNARE complexes.
Lupashin et al., Little Rock, United States. In Nat Commun, 2012
Here, using yeast two-hybrid and co-immunoprecipitation approaches, we show that three COG subunits, namely COG4, 6 and 8, are capable of interacting with defined Golgi SNAREs, namely STX5, STX6, STX16, GS27 and SNAP29.
Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery.
Lupashin et al., Little Rock, United States. In Glycobiology, 2011
MALDI-TOF analysis of total N-linked glycoconjugates indicated a decrease in the relative amount of sialylated glycans in both COG3 KD and COG4 KD cells.
Identification of the first COG-CDG patient of Indian origin.
Freeze et al., Los Angeles, United States. In Mol Genet Metab, 2011
Here we present data identifying a previously reported CDG-IIx case from Singapore as a new COG4 patient with 2 novel mutations leading to p.E233X and p.L773R; with p.E233X being a de novo mutation.
Molecular organization of the COG vesicle tethering complex.
Hughson et al., Princeton, United States. In Nat Struct Mol Biol, 2010
To begin elucidating the molecular architecture of one well-studied example, the conserved oligomeric Golgi (COG) complex, we reconstituted its essential subunits (Cog1, Cog2, Cog3 and Cog4) and used single-particle electron microscopy to reveal a y-shaped structure with three flexible, highly extended legs.
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.
Golgi function and dysfunction in the first COG4-deficient CDG type II patient.
Matthijs et al., Leuven, Belgium. In Hum Mol Genet, 2009
A novel R729W missense mutation in COG4 was associated with the congenital disorder of glycosylation type II.
Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene.
Hughson et al., Princeton, United States. In Proc Natl Acad Sci U S A, 2009
The 1.9 A crystal structure of a Cog4 C-terminal fragment, was determined. Arg 729 is found to occupy a key position at the center of a salt bridge network, thereby stabilizing Cog4's small C-terminal domain.
Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing.
Lev et al., Israel. In Embo J, 2009
Study shows that the SM protein, Sly1, interacts directly with the conserved oligomeric Golgi (COG) tethering complex; Sly1-COG interaction is mediated by the Cog4 subunit, which also interacts with Syntaxin 5 through a different binding site.
Large scale screening for novel rab effectors reveals unexpected broad Rab binding specificity.
Itoh et al., Sendai, Japan. In Mol Cell Proteomics, 2008
INPP5E and Cog4) with a specific Rab isoform was confirmed by co-immunoprecipitation assay and/or colocalization analysis in mammalian cell cultures, and the novel Rab2B-binding domain of Golgi-associated Rab2B interactor (GARI) and GARI-like proteins was identified by deletion and homology search analyses.
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