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MetabolomicsGolgi-IP, a tool for multimodal analysis of Golgi molecular content
The Golgi is a membrane-bound organelle that is essential for protein and lipid biosynthesis. It represents a central trafficking hub that sorts proteins and lipids to various destinations or for secretion from the cell. The Golgi has emerged as a docking platform for cellular signaling pathways inc...
2023-06-27 | MTBLS6511 | MetaboLights
MetabolomicsAnalysis of short chain phosphatidylcholine (PC) on the Golgi membrane
Not available
ORGANISM(S): Cricetulus griseus 
ST001177 | MetabolomicsWorkbench
MetabolomicsNPC1 regulates the distribution of phosphatidylinositol 4 kinases at Golgi and Lysosome membranes
Cholesterol and phosphoinositides (PI) are two critically important lipids that are found in cellular membranes and dysregulated in many disorders. Therefore, uncovering molecular pathways connecting these essential lipids may offer new therapeutic insights. We report that loss of function of lysoso...
2021-09-15 | MTBLS2612 | MetaboLights
MetabolomicsInositol triphosphate-triggered calcium release blocks lipid exchange at endoplasmic reticulum-Golgi contact sites
Vesicular traffic and membrane contact sites between organelles enable the exchange of proteins, lipids, and metabolites. Recruitment of membrane tethers to contact sites between the endoplasmic reticulum (ER) and the plasma membrane is often triggered by calcium. In contrast, we reveal here a funct...
2021-05-06 | MTBLS2444 | MetaboLights
ProteomicsTrans-Golgi protein TVP23B regulates host-microbe interactions via Paneth cell homeostasis and Goblet cell glycosylation
A key feature in intestinal immunity is the dynamic intestinal barrier, which separates the host from resident and pathogenic microbiota through a mucus gel impregnated with antimicrobial peptides. The mechanisms underlying the maintenance and function of this intestinal barrier are not completely ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2022-12-12 | MSV000090883 | MassIVE
GenomicsDe novo Golgi biogenesis requires orchestrated transactivation of Golgi genes
De novo Golgi biogenesis requires orchestrated transactivation of Golgi genes
PRJNA1217352 | ENA
ProteomicsDissecting the secretory pathway with electrophoresis reveals intra-Golgi trafficking pathways and enables compilation of sub-Golgi and sub-ER proteomes.
The Golgi is the hub of the eukaryotic secretory pathway, trafficking proteins and lipids, as well as synthesizing complex sugars. Different biosynthetic reactions are associated with different compartments of its complex architecture. Although pre- and post-Golgi trafficking has been much studied...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-09-11 | PXD004596 | Pride
Arabidopsis Free flow electrophoresis Proteomics Trans-membrane span Secretory pathway Polysaccharide Endoplasmic reticulum Trafficking Golgi Cisternae Immunogold 
ProteomicsCOG complex-dependent Golgi-derived vesicles from hTERT-RPE1 cells EXP1
Intracellular trafficking relies on small vesicular intermediates, though their specific role in Golgi function is still debated. To clarify this, we induced acute dysfunction of the Conserved Oligomeric Golgi (COG) complex and analyzed vesicles from cis, medial, and trans-Golgi compartments. Proteo...
ORGANISM(S): Homo sapiens (Human) 
2026-08-31 | PXD057633 | Pride
Glycosylation Golgi Vesicle Cog complex Immunoprecipitation Human 
TranscriptomicsAn integrated global analysis of compartmentalized HRAS signaling
Modern omics technologies allow us obtaining global information on different types of biological networks. However, integrating these different types of analyzes into a coherent framework for a comprehensive biological interpretation remains challenging. Here, we present a conceptual framework that ...
ORGANISM(S): Homo sapiens 
2019-03-12 | E-MTAB-7672 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of yeast expressing mouse major histocompatibility complex class I heavy chain H-2K(b)
To dissect the requirements of membrane protein degradation from the ER, we expressed the mouse major histocompatibility complex class I heavy chain H-2K(b) in yeast. Like other proteins degraded from the ER, unassembled H-2K(b) heavy chains are not transported to the Golgi but are degraded in a pro...
ORGANISM(S): Saccharomyces cerevisiae 
2005-06-28 | E-SMDB-1576 | biostudies-arrayexpress
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