ReviewJournal of molecular biology2016
Glycosylation Quality Control by the Golgi Structure.
Review in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
76 citing papers in PubMed.
- A USP28-TM9SF3-Golgiphagy axis maintains glycosylation homeostasis and promotes breast cancer progression.The EMBO journal · 2026Article
- α-mannosidase I-dependent N-linked glycosylation affects hERG channel functional availability during reactivation.The journal of physiological sciences : JPS · 2026Article
- Glycogen and Glycosylation: Friends or Foes?Biomolecules · 2026Review
- Tjap1/Pilt Is a cis-Golgi-Associated Protein Required for Golgi Integrity and Normal Drug Transporter Expression in Brain Microvascular Endothelial Cells In Vitro.Pharmaceutics · 2026Article
- AXL receptor tyrosine kinase regulates Golgi organization and function via an adhesion-Arf1 signalling axis in breast and lung cancer cell lines.Biology open · 2026Article
- Golgi Fragmentation as a Potential Link Between SARS-CoV-2 Infection and Alzheimer's Disease: Mechanisms and Implications for Neurodegeneration in Long COVID.Sub-cellular biochemistry · 2026Review
- Selective Paracrine Modulation of Stromal Cells: Wharton's Jelly MSC Secretome Enhances Adipose-Derived MSC Functionality While Maintaining Dermal Fibroblast Quiescence.International journal of molecular sciences · 2025Article
- Multiple golgins are required to support extracellular matrix secretion, modification, and assembly.The Journal of cell biology · 2025Article
- WW Domain-Containing E3 Ubiquitin Protein Ligase 1 (WWP1) as a Factor in Obesity-Related Metabolic Disorders: Emerging Molecular Mechanisms in Metabolic Tissues.International journal of molecular sciences · 2025Review
- SARS-CoV-2 remodels the Golgi apparatus to facilitate viral assembly and secretion.PLoS pathogens · 2025Article
- Glycosylation as an intricate post-translational modification process takes part in glycoproteins related immunity.Cell communication and signaling : CCS · 2025Review
- Lysophosphatidylcholine promoting α-Synuclein aggregation in Parkinson's disease: disrupting GCase glycosylation and lysosomal α-Synuclein degradation.NPJ Parkinson's disease · 2025Article
- GRASP55 regulates sorting and maturation of the lysosomal enzyme β-hexosaminidase A.Molecular biology of the cell · 2025Article
- Article
- H5 subtype avian influenza virus induces Golgi apparatus stress response via TFE3 pathway to promote virus replication.PLoS pathogens · 2024Article
- The effects of WWP1 overexpression on the golgi apparatus stress response and proteoglycan production in adipocytes.Scientific reports · 2024Article
- GDNF improves the cognitive ability of PD mice by promoting glycosylation and membrane distribution of DAT.Scientific reports · 2024Article
- GolpHCat (TMEM87A), a unique voltage-dependent cation channel in Golgi apparatus, contributes to Golgi-pH maintenance and hippocampus-dependent memory.Nature communications · 2024Article
- Protein networking: nicotinic acetylcholine receptors and their protein-protein-associations.Molecular and cellular biochemistry · 2024Review
- Morphological determination of localization and function of Golgi proteins.Biophysics reports · 2024Article
16 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Glycosylation is a ubiquitous modification that occurs on proteins and lipids in all living cells. Consistent with their high complexity, glycans play crucial biological roles in protein quality control and recognition events. Asparagine-linked protein N-glycosylation, the most complex glycosylation, initiates in the endoplasmic reticulum and matures in the Golgi apparatus. This process not only requires an accurate distribution of processing machineries, such as glycosyltransferases, glycosidases, and nucleotide sugar transporters, but also needs an efficient and well-organized factory that is responsible for the fidelity and quality control of sugar chain processing. In addition, accurate glycosylation must occur in coordination with protein trafficking and sorting. These activities are carried out by the Golgi apparatus, a membrane organelle in the center of the secretory pathway. To accomplish these tasks, the Golgi has developed into a unique stacked structure of closely aligned, flattened cisternae in which Golgi enzymes reside; in mammalian cells, dozens of Golgi stacks are often laterally linked into a ribbon-like structure. Here, we review our current knowledge of how the Golgi structure is formed and why its formation is required for accurate glycosylation, with the focus on how the Golgi stacking factors GRASP55 and GRASP65 generate the Golgi structure and how the conserved oligomeric Golgi complex maintains Golgi enzymes in different Golgi subcompartments by retrograde protein trafficking.
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