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Search Results to Vladimir Lupashin

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One or more keywords matched the following properties of Lupashin, Vladimir

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overview Our laboratory is interested in understanding the molecular mechanisms responsible for the generation and maintenance of intra-cellular membrane-bounded compartments. In all eukaryotic cells intracellular membrane trafficking is critical for a range of important cellular functions including protein secretion, post-translational modifications, cell signalling, cell polarization, and cell maintenance. Defects in membrane trafficking can underline, or even exacerbate, a number of human diseases including cancer, diabetes mellitus, Alzheimer’s, cystic fibrosis, Hermansky-Pudlak syndrome and Congenital Disorders of Glycosylation. Our research directed towards the understanding of the basic mechanisms of intracellular vesicular trafficking using both yeast and mammalian tissue culture cell model systems. Our lab played a principal role in the discovery of a novel vesicle tethering factors, published more than 60 original papers in high-profile journals, including Journal of Cell Biology, PNAS, Science, Journal of Neuroscience, Molecular Biology of Cell and Nature Communications. My current research has been continuously supported by grants from both NSF and NIH. We have pioneered the functional analysis of the Conserved Oligomeric Golgi (COG), an evolutionarily conserved complex of eight gene products, each of which is critical for the membrane trafficking and protein modifications in the Golgi apparatus. The COG complex interacts with core fusion machinery components including SNAREs, SM proteins, Rabs, coiled-coil tethers and COPI coat to organize specific docking and fusion of transport intermediates with their acceptor membrane. By using state of the art biochemical, genetic and microscopy approaches (including mass-spectrometry, electron and super-resolution microscopy, CRISPR directed gene editing techniques) we would like to determine how the key components of intracellular membrane trafficking machinery work together to direct efficient protein trafficking in human cells in health and disease.

One or more keywords matched the following items that are connected to Lupashin, Vladimir

Item TypeName
Academic Article Cog1p plays a central role in the organization of the yeast conserved oligomeric Golgi complex.
Academic Article Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability.
Academic Article Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells.
Academic Article Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs.
Academic Article COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation.
Academic Article COG complexes form spatial landmarks for distinct SNARE complexes.
Academic Article COG6 interacts with a subset of the Golgi SNAREs and is important for the Golgi complex integrity.
Academic Article The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins.
Concept SNARE Proteins
Concept Qc-SNARE Proteins
Concept Qa-SNARE Proteins
Academic Article Identification and characterization of novel proteins involved in the regulation of SNARE-complex assembly
Academic Article Yeast COG complex, a Ypt1 effector required for retrograde intra-Golgi trafficking COG interacts with the Golgi SNAREs and with COPI vesicle coat proteins
Academic Article Uso1p is required for assembly of the ER to Golgi SNARE complex
Academic Article In vivo and in vitro analysis of ER to Golgi SNARE complex assembly in yeast
Academic Article The COG Complex regulates intra-Golgi cycling of vesicles that carry SNAREs and glycosyltransferases
Academic Article The COG complex interacts with the t-SNARE Syntaxin5 to direct trafficking of recyling intra-Golgi vesicles that is essential for normal protein glycosylation
Academic Article The COG complex interacts with Syntaxin5a to stabilize intra-Golgi SNARE complex and to direct trafficking of recycling intra-Golgi vesicles
Academic Article The Conserved Oligomeric Golgi complex functional interaction with SNARE and Rab proteins
Academic Article The Conserved Oligomeric Golgi complex directly interacts with the t-SNARE Syntaxin5/Sed5 and regulates formation of the intra-Golgi SNARE complex
Academic Article COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex.
Academic Article Creating Knockouts of Conserved Oligomeric Golgi Complex Subunits Using CRISPR-Mediated Gene Editing Paired with a Selection Strategy Based on Glycosylation Defects Associated with Impaired COG Complex Function.
Grant Characterization of mammalian COG complex-interacting Golgi trafficking machinery
Academic Article Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation.

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  • SNARE Proteins