Author

V. Lupashin

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Cell Biology· 4

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 4 Approach:experimental assay· 4 Organism:human· 4 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 1 Research Focus:cell-cell communication· 1 Research Focus:clustering· 1 Research Focus:differential expression· 1

Frequent Co-Authors

Z. D'Souza· 3 shared A. Khakurel· 2 shared I. D. Pokrovskaya· 2 shared F. S. Taher· 1 shared I. Pokrovskaya· 1 shared J. S. Bonifacino· 1 shared T. A. Kudlyk· 1 shared T. Kudlyk· 1 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

8 top collaborators · 12 mutual co-author links

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3 shared papersCell Biology

Z. D'Souza

Mutual co-authors in cluster

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4 papers

Recent·Most cited

GARP complex controls Golgi physiology by stabilizing COPI machinery and Golgi v-SNAREs

A. Khakurel, T. Kudlyk, I. Pokrovskaya, Z. D'Souza, V. Lupashin

This study investigates the role of the GARP complex in Golgi physiology, showing it stabilizes COPI machinery and v-SNAREs, and its depletion causes Golgi structural and functional defects.

bioRxiv · Jul 22, 2022 · PreprintCell Biology

Acute COG inactivation unveiled its immediate impact on Golgi and illuminated the nature of intra-Golgi recycling vesicles

F. S. Taher, I. D. Pokrovskaya, Z. D'Souza, V. Lupashin

This study uses acute COG inactivation to reveal the immediate effects on Golgi structure and intra-Golgi recycling vesicles in human cells.

bioRxiv · May 24, 2022 · PreprintCell Biology

STX5's flexibility in SNARE pairing supports Golgi functions

Z. D'Souza, I. D. Pokrovskaya, V. Lupashin

This study investigates the role of STX5 in Golgi function by analyzing SNARE pairing flexibility in COG complex-deficient cells, revealing non-canonical SNARE complexes that compensate for COG dysfunction.

bioRxiv · May 24, 2022 · PreprintCell Biology

The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery

A. Khakurel, T. A. Kudlyk, J. S. Bonifacino, V. Lupashin

This study shows that the GARP complex is essential for maintaining Golgi glycosylation by stabilizing enzymes and preventing their mislocalization to endolysosomes.

bioRxiv · Dec 21, 2020Cell Biology