Vladimir Lupashin
Professor
faculty
Physiology & Cell Biology, College of Medicine
Research Areas
Biography and Research Information
OverviewAI-generated summary
Vladimir Lupashin's research laboratory focuses on elucidating the molecular mechanisms underlying the generation and maintenance of intracellular membrane-bounded compartments. Intracellular membrane trafficking is essential for numerous cellular functions, including protein secretion, post-translational modifications, cell signaling, polarization, and maintenance. Disruptions in this process are implicated in various human diseases such as cancer, diabetes mellitus, Alzheimer's disease, cystic fibrosis, Hermansky-Pudlak syndrome, and Congenital Disorders of Glycosylation.
Lupashin's laboratory employs both yeast and mammalian tissue culture cell models to investigate the fundamental mechanisms of intracellular vesicular trafficking. His work has contributed to the discovery of novel vesicle tethering factors. He has authored over 125 publications, with a h-index of 42 and over 5,200 citations, appearing in journals such as the Journal of Cell Biology, PNAS, Science, Journal of Neuroscience, Molecular Biology of the Cell, and Nature Communications. His research has been supported by continuous funding from the NSF and NIH, including a recent NIH/National Institute of General Medical Sciences grant totaling $409,543 for the characterization of mammalian COG complex-interacting Golgi trafficking machinery, with Lupashin serving as PI.
His current research investigates the role of the Golgi-associated retrograde protein (GARP) complex in maintaining Golgi glycosylation machinery and the function of the conserved oligomeric Golgi (COG) complex in various cellular models, including those relevant to CDG-II diseases. He also studies the role of syntaxin-5 in SNARE pairing for Golgi functions and the impact of COG complex inactivation on Golgi physiology and intra-Golgi recycling vesicles. Collaborations within the University of Arkansas for Medical Sciences include work with 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: 5,297
Selected Publications
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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)
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Correction to: Golgi (2023)
Federal Grants 1 $409,543 total
Characterization of mammalian COG complex-interacting Golgi trafficking machinery
Grants & Funding
- Remodeling of intracellular membrane traffic by Brucella effectors- Washington State Sub NIH/Nat. Inst. of Allergy & Infectious Diseases - Pass Through: Washington State University Principal Investigator
- COM-Intramural Award UAMS College of Medicine Principal Investigator
- Remodeling of intracellular membrane traffic by Brucella effectors- Washington State Sub NIH/Nat. Inst. of Allergy & Infectious Diseases - Pass Through: Washington State University 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
- Characterization of mammalian COG complex-interacting Golgi trafficking machinery NIH Principal Investigator
- Characterization of mammalian COG complex-interacting Golgi trafficking machinery NIH/Nat. Inst. of General Medical Sciences Principal Investigator
- Functional Analysis of the conserved oligomeric Golgi (COG) complex in yeast National Science Foundation Principal Investigator
Collaboration Network
Top Collaborators
- 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 11 shared publications
- 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 10 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 8 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
- STX5’s flexibility in SNARE pairing supports Golgi functions
- GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
Showing 5 of 7 shared publications
- Comprehensive Proteomic Characterization 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
- Author response for "Acute <scp>GARP</scp> Depletion Disrupts Vesicle Transport, Leading to Severe Defects in Sorting, Secretion and <i>O</i>‐Glycosylation"
- Author response for "Acute <scp>GARP</scp> Depletion Disrupts Vesicle Transport, Leading to Severe Defects in Sorting, Secretion and <i>O</i>‐Glycosylation"
- Deep proteomic profiling of the intra-Golgi trafficking intermediates
- 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
- 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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