Vladimir Lupashin
Professor
Also affiliated: Dartmouth College (1998); University of North Carolina at Chapel Hill (2020); Russian Academy of Sciences (1987); National Research Tomsk State University (2014); Siberian State Medical University (2014); Princeton University (1996–1999); University of Arkansas Medical Center (2013–2022); Institute of Biochemistry and Physiology of Plants and Microorganisms (1992); Institute of Protein Research (1992); G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms (1987–1992); Institute of Mathematical Problems of Biology (1992); Arkansas Department of Agriculture (2014); University of California, Berkeley (1996)
Faculty Researcher
Physiology & Cell Biology, College of Medicine
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Vladimir Lupashin's research focuses on the molecular mechanisms underlying the generation and maintenance of intracellular membrane-bounded compartments. His work investigates intracellular vesicular trafficking, utilizing both yeast and mammalian tissue culture cell model systems. This research is critical for understanding cellular functions such as protein secretion, post-translational modifications, cell signaling, cell polarization, and cell maintenance. Defects in membrane trafficking are implicated in a range of human diseases, including cancer, diabetes mellitus, Alzheimer’s disease, cystic fibrosis, Hermansky-Pudlak syndrome, and Congenital Disorders of Glycosylation.
Dr. Lupashin's laboratory has played a significant role in the discovery of novel vesicle tethering factors. He has published over 125 original papers in journals such as the *Journal of Cell Biology*, *PNAS*, *Science*, *Journal of Neuroscience*, *Molecular Biology of Cell*, and *Nature Communications*. His research has been consistently supported by grants from the NSF and NIH, including a current NIH/National Institute of General Medical Sciences grant for $409,543 to characterize mammalian COG complex-interacting Golgi trafficking machinery. He holds an h-index of 42 and has accumulated over 5,300 citations.
His recent publications highlight the essential role of the Golgi-associated retrograde protein (GARP) complex in maintaining Golgi glycosylation machinery and the broader physiological functions of the GARP vesicle tethering complex. Other work examines the flexibility of Syntaxin-5 in SNARE pairing for Golgi functions, the impact of acute COG complex inactivation on Golgi activity, and the differential effects of COG complex subunit deficiency on proteoglycan synthesis. Dr. Lupashin also leads a research group and collaborates with colleagues at the University of Arkansas for Medical Sciences, including Irina D. Pokrovskaya, Amrita Khakurel, Farhana Taher Sumya, and Zinia D’Souza.
Research 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.
Metrics
- h-index: 42
- Publications: 125
- Citations: 5,408
Selected Publications
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Golgi CATCHR complexes function as organizing hubs for vesicle tethering and fusion (2026)
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COG Complex in Golgi Trafficking and Glycosylation (2026)
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GARP Complex in Golgi Physiology (2026)
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Deep proteomic profiling of the intra-Golgi trafficking intermediates (2025)
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Acute <scp>GARP</scp> Depletion Disrupts Vesicle Transport, Leading to Severe Defects in Sorting, Secretion and <i>O</i> ‐Glycosylation (2025)
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Comprehensive Proteomic Characterization of the Intra-Golgi Trafficking Intermediates (2024)
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Acute GARP depletion disrupts vesicle transport, leading to severe defects in sorting, secretion, and O-glycosylation (2024)
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Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i> (2023)
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Biallelic missense variants in <scp><i>COG3</i></scp> cause a congenital disorder of glycosylation with impairment of retrograde vesicular trafficking (2023)
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Syntaxin‐5's flexibility in <scp>SNARE</scp> pairing supports Golgi functions (2023)
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A Rab33b missense mouse model for Smith-McCort dysplasia shows bone resorption defects and altered protein glycosylation (2023)
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Essential role of the Conserved Oligomeric Golgi complex in <i>Toxoplasma gondii</i> (2023)
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Faculty Opinions recommendation of The K/HDEL receptor does not recycle but instead acts as a Golgi-gatekeeper. (2023)
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Insights into the regulation of cellular Mn2+ homeostasis via TMEM165 (2023)
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Role of GARP Vesicle Tethering Complex in Golgi Physiology (2023)
Federal Grants 1 $409,543 total
Characterization of mammalian COG complex-interacting Golgi trafficking machinery
Grants & Funding
As listed on this researcher's institutional profile. Federal awards with verified records are shown above.
- Remodeling of intracellular membrane traffic by Brucella effectors- Washington State Sub NIH/Nat. Inst. of Allergy & Infectious Diseases via Washington State University Principal Investigator
- COM-Intramural Award UAMS College of Medicine Principal Investigator
- Functional Analysis of the conserved oligomeric Golgi (COG) complex in yeast National Science Foundation Principal Investigator
- Structural and functional analysis of SEC 34 Protein complex National Science Foundation Principal Investigator
- Super-Res Holographic Microscopy to Advance Research on Golgi Apparatus Function NIH Co-Investigator
- Role of COG complex mediated vesicle tethering is localization of Golgi enzymes Mizutani Foundation for Glycoscience Principal Investigator
- Super-Resolution Light Microscope at University of Arkansas for Medical Sciences NIH Co-Investigator
- Modulation of host secretory trafficking by the Brucella effector BspB - Continuation - Continuation NIH/Nat. Inst. of General Medical Sciences via Washington State University Principal Investigator
Collaboration Network
Top Collaborators
- The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery
- Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation
- Role of GARP Vesicle Tethering Complex in Golgi Physiology
- GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
- Generation and Analysis of hTERT-RPE1 VPS54 Knock-Out and Rescued Cell Lines
Showing 5 of 9 shared publications
- Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation
- Development and Initial Characterization of Cellular Models for COG Complex-Related CDG-II Diseases
- Acute COG complex inactivation unveiled its immediate impact on Golgi and illuminated the nature of intra‐Golgi recycling vesicles
- Biallelic missense variants in <scp><i>COG3</i></scp> cause a congenital disorder of glycosylation with impairment of retrograde vesicular trafficking
- Rapid COG Depletion in Mammalian Cell by Auxin-Inducible Degradation System
Showing 5 of 9 shared publications
- Development and Initial Characterization of Cellular Models for COG Complex-Related CDG-II Diseases
- Acute COG complex inactivation unveiled its immediate impact on Golgi and illuminated the nature of intra‐Golgi recycling vesicles
- Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- STX5’s flexibility in SNARE pairing supports Golgi functions
- Rapid COG Depletion in Mammalian Cell by Auxin-Inducible Degradation System
Showing 5 of 9 shared publications
- Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation
- Syntaxin‐5's flexibility in <scp>SNARE</scp> pairing supports Golgi functions
- Acute COG complex inactivation unveiled its immediate impact on Golgi and illuminated the nature of intra‐Golgi recycling vesicles
- GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
- STX5’s flexibility in SNARE pairing supports Golgi functions
Showing 5 of 7 shared publications
- The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery
- GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
- Generation and Analysis of hTERT-RPE1 VPS54 Knock-Out and Rescued Cell Lines
- GARP complex controls Golgi physiology by stabilizing COPI machinery and Golgi v-SNAREs
- Syntaxin‐5's flexibility in <scp>SNARE</scp> pairing supports Golgi functions
- GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
- Acute GARP depletion disrupts vesicle transport, leading to severe defects in sorting, secretion, and O-glycosylation
- GARP complex controls Golgi physiology by stabilizing COPI machinery and Golgi v-SNAREs
- Comprehensive Proteomic Characterization of the Intra-Golgi Trafficking Intermediates
- Deep proteomic profiling of the intra-Golgi trafficking intermediates
- Acute <scp>GARP</scp> Depletion Disrupts Vesicle Transport, Leading to Severe Defects in Sorting, Secretion and <i>O</i> ‐Glycosylation
- Golgi
- Correction to: Golgi
- Golgi
- Correction to: Golgi
- Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the Conserved Oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the Conserved Oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the Conserved Oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the Conserved Oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Essential role of the Conserved Oligomeric Golgi complex in <i>Toxoplasma gondii</i>
- Proteoglycan synthesis in conserved oligomeric Golgi subunit deficient <scp>HEK293T</scp> cells is affected differently, depending on the lacking subunit
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