ReviewFrontiers in cell and developmental biology2019
The Physiological Functions of the Golgin Vesicle Tethering Proteins.
Review in Frontiers in cell and developmental biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- UBA1 knockdown dysregulates UBA1-sensitive proteins and impairs muscle function in models of spinal muscular atrophy X-linked 2.Disease models & mechanisms · 2026Article
- Physiological implications of phase separation in vesicle organization and trafficking.BMC biology · 2026Review
- Protein Kinase D2 Regulates GRASP65 Phosphorylation and Golgi Ribbon Unlinking During G2/M Transition.Cells · 2026Article
- Plant Golgi and GECCO: The Universality of ER-Golgi Interface.Sub-cellular biochemistry · 2026Review
- The Functions of the Golgin Family of Coiled-Coil Proteins.Sub-cellular biochemistry · 2026Review
- The Impact of Golgi Organization on Cell Cycle and Cancer Development.Sub-cellular biochemistry · 2026Review
- RME-1-associated recycling endosomes participate in vitellogenin secretion inLife metabolism · 2025Article
- Multiple golgins are required to support extracellular matrix secretion, modification, and assembly.The Journal of cell biology · 2025Article
- Glycerol mediates crosstalk between metabolism and trafficking through the golgin Imh1.Nature structural & molecular biology · 2025Article
- Alternative splicing controls pan-neuronal homeobox gene expression.Genes & development · 2025Article
- The FAM114A proteins are adaptors for the recycling of Golgi enzymes.Journal of cell science · 2024Article
- The Golgi checkpoint: Golgi unlinking during G2 is necessary for spindle formation and cytokinesis.Life science alliance · 2024Article
- Cargo selective vesicle tethering: The structural basis for binding of specific cargo proteins by the Golgi tether component TBC1D23.Science advances · 2024Article
- The role of Golgi complex proteins in cell division and consequences of their dysregulation.Frontiers in cell and developmental biology · 2024Review
- GOLGA8 increases bulk antisense oligonucleotide uptake and activity in mammalian cells.Molecular therapy. Nucleic acids · 2023Article
- Out of the ESCPE room: Emerging roles of endosomal SNX-BARs in receptor transport and host-pathogen interaction.Traffic (Copenhagen, Denmark) · 2023Review
- From Cell to Symptoms: The Role of SARS-CoV-2 Cytopathic Effects in the Pathogenesis of COVID-19 and Long COVID.International journal of molecular sciences · 2023Review
- Hyaluronan in the Cancer Cells Microenvironment.Cancers · 2023Review
- Golgi Complex form and Function: A Potential Hub Role Also in Skeletal Muscle Pathologies?International journal of molecular sciences · 2022Article
- In vivo characterization of Drosophila golgins reveals redundancy and plasticity of vesicle capture at the Golgi apparatus.Current biology : CB · 2022Article
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1 author.
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Abstract
The golgins comprise a family of vesicle tethering proteins that act in a selective manner to tether transport vesicles at the Golgi apparatus. Tethering is followed by membrane fusion to complete the delivery of vesicle-bound cargo to the Golgi. Different golgins are localized to different regions of the Golgi, and their ability to selectively tether transport vesicles is important for the specificity of vesicle traffic in the secretory pathway. In recent years, our mechanistic understanding of golgin-mediated tethering has greatly improved. We are also beginning to appreciate how the loss of golgin function can impact upon physiological processes through the use of animal models and the study of human disease. These approaches have revealed that loss of a golgin causes tissue-restricted phenotypes, which can vary in severity and the cell types affected. In many cases, it is possible to attribute these phenotypes to a defect in vesicular traffic, although why certain tissues are sensitive to loss of a particular golgin is still, in most cases, unclear. Here, I will summarize recent progress in our understanding of golgins, focusing on the physiological roles of these proteins, as determined from animal models and the study of disease in humans. I will describe what these
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