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Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function
Consideration of biochemical and genetic data for mammalian COG and its yeast homologue suggests a model for the subunit distribution within this complex, which plays critical roles in Golgi structure and function. Expand
The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins.
COG and COPI may work in concert to ensure the proper retention or retrieval of a subset of proteins in the Golgi, and COG helps prevent the endoplasmic reticulum accumulation and degradation of some GEARs. Expand
COG complexes form spatial landmarks for distinct SNARE complexes
Using yeast two hybrid and co-immunoprecipitation approaches, it is shown that three COG subunits, namely COG4, 6, and 8, are capable of interacting with defined Golgi SNAREs, namely STX5,STX6, STX16, GS27, and SNAP29. Expand
SNARE protein structure and function.
  • D. Ungar, F. Hughson
  • Biology, Medicine
  • Annual review of cell and developmental biology
  • 28 November 2003
The SNARE superfamily has become, since its discovery approximately a decade ago, the most intensively studied element of the protein machinery involved in intracellular trafficking and there is still much to learn about how the assembly and activity of this machinery is choreographed in living cells. Expand
A new inborn error of glycosylation due to a Cog8 deficiency reveals a critical role for the Cog1-Cog8 interaction in COG complex formation.
A patient with a mild form of a congenital disorder of glycosylation type II (CDG-II) is described, which is caused by a homozygous nonsense mutation in the hCOG8 gene, resulting in a truncated Cog8 subunit lacking the 76 C-terminal amino acids. Expand
Subunit Architecture of the Conserved Oligomeric Golgi Complex*
The conserved oligomeric Golgi (COG) complex is thought to function in intra-Golgi retrograde trafficking mediated by coat protein I vesicles, a pathway essential for the proper structure andExpand
COG8 deficiency causes new congenital disorder of glycosylation type IIh.
Lentiviral-mediated complementation with normal COG8 corrected mislocalization of other COG proteins, normalized sialylation and restored normal BFA-induced Golgi disruption. Expand
Retrograde transport on the COG railway.
This hypothesis explains the impact of COG mutations by postulating that they impair the retrograde flow of resident Golgi proteins needed to maintain normal Golgi structure and function. Expand
Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation.
Retroviral complementation of the patients' fibroblasts with the wild-type COG6-cDNA led to normalization of the COG complex-depending retrograde protein transport after Brefeldin A treatment, demonstrated by immunofluorescence analysis. Expand
Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene
Study in HeLa cells reveal that Cog4 bears a strong structural resemblance to exocyst and Dsl1p complex subunits; the emerging structural similarities provide strong evidence of a common evolutionary origin and may reflect shared mechanisms of action. Expand