ArticleProceedings of the National Academy of Sciences of the United States of America2009
Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 64 citations in OpenAlex.
- COG Complex in Golgi Trafficking and Glycosylation.Sub-cellular biochemistry · 2026Review
- Deep learning-based assessment of missense variants in theBMJ open ophthalmology · 2025Article
- Structure of a membrane tethering complex incorporating multiple SNAREs.Nature structural & molecular biology · 2024Article
- Whole-Exome Sequencing in a Family with an Unexplained Tendency for Venous Thromboembolism: Multicomponent Prediction of Low-Frequency Variant Deleteriousness and of Individual Protein Interaction.International journal of molecular sciences · 2023Article
- Acute COG complex inactivation unveiled its immediate impact on Golgi and illuminated the nature of intra-Golgi recycling vesicles.Traffic (Copenhagen, Denmark) · 2023Article
- Homology and Modular Evolution of CATCHR at the Origin of the Eukaryotic Endomembrane System.Genome biology and evolution · 2021Article
- Development and Initial Characterization of Cellular Models for COG Complex-Related CDG-II Diseases.Frontiers in genetics · 2021Article
- Golgi inCOGnito: From vesicle tethering to human disease.Biochimica et biophysica acta. General subjects · 2020Review
- Cog4 is required for protrusion and extension of the epithelium in the developing semicircular canals.Mechanisms of development · 2019Article
- Exposing the Elusive Exocyst Structure.Trends in biochemical sciences · 2018Review
- More than just sugars: Conserved oligomeric Golgi complex deficiency causes glycosylation-independent cellular defects.Traffic (Copenhagen, Denmark) · 2018Article
- Membrane detachment is not essential for COG complex function.Molecular biology of the cell · 2018Article
- Conserved Oligomeric Golgi and Neuronal Vesicular Trafficking.Handbook of experimental pharmacology · 2018Review
- Crystal structure of Sec10, a subunit of the exocyst complex.Scientific reports · 2017Article
- Distinct Roles for the N- and C-terminal Regions of M-Sec in Plasma Membrane Deformation during Tunneling Nanotube Formation.Scientific reports · 2016Article
- Molecular architecture of the complete COG tethering complex.Nature structural & molecular biology · 2016Article
- CATCHR, HOPS and CORVET tethering complexes share a similar architecture.Nature structural & molecular biology · 2016Article
- COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex.Scientific reports · 2016Article
- The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase.eLife · 2016Article
- COG Complex Complexities: Detailed Characterization of a Complete Set of HEK293T Cells Lacking Individual COG Subunits.Frontiers in cell and developmental biology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The proper glycosylation of proteins trafficking through the Golgi apparatus depends upon the conserved oligomeric Golgi (COG) complex. Defects in COG can cause fatal congenital disorders of glycosylation (CDGs) in humans. The recent discovery of a form of CDG, caused in part by a COG4 missense mutation changing Arg 729 to Trp, prompted us to determine the 1.9 A crystal structure of a Cog4 C-terminal fragment. 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. Studies in HeLa cells reveal that this C-terminal domain, while not needed for the incorporation of Cog4 into COG complexes, is essential for the proper glycosylation of cell surface proteins. We also find that Cog4 bears a strong structural resemblance to exocyst and Dsl1p complex subunits. These complexes and others have been proposed to function by mediating the initial tethering between transport vesicles and their membrane targets; the emerging structural similarities provide strong evidence of a common evolutionary origin and may reflect shared mechanisms of action.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.