Author

O. Kovtun

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

Biology Disciplines

Click to filter author papers

Cell Biology· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:imaging· 1 Assay:protein sequence· 1 Assay:protein structure· 1 Assay:structural biology· 1

Frequent Co-Authors

B. M. Collins· 2 shared N. Ariotti· 2 shared A. G. Wrobel· 1 shared A. Mayer· 1 shared B. T. Kelly· 1 shared D. J. Owen· 1 shared F. Sroubek· 1 shared J. A. G. Briggs· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersCell Biology

B. M. Collins

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Molecular basis for the assembly of the Vps5-Vps17 SNX-BAR proteins with Retromer

K.-E. Chen, V. A. Tillu, N. Gopaldass, S. R. Chowdhury, N. Leneva, O. Kovtun, J. Ruan, Q. Guo, N. Ariotti, A. Mayer, B. M. Collins

This study investigates how Vps5 and Vps17 SNX-BAR proteins assemble with Retromer, revealing a PL motif in Vps5 that binds Vps29 and is essential for membrane tubule association and cargo recycling.

bioRxiv · Mar 24, 2024Cell Biology

FCHO controls AP2's critical endocytic roles through a PtdIns4,5P2 membrane-dependent switch

N. R. Zaccai, Z. Kadlecova, V. Kane Dickson, K. Korobchevskaya, J. Kamenicky, O. Kovtun, P. K. Umasankar, A. G. Wrobel, J. G. G. Kaufman, S. R. Gray, K. Qu, P. R. Evans, M. Fritzsche, F. Sroubek, S. Höning, , L. M. Traub

The paper shows FCHO primes AP2 for clathrin-coated vesicle incorporation, triggering FCHO release to enable further AP2 activation and recruitment.

bioRxiv · Apr 2, 2022 · PreprintCell Biology

Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation

V. Tillu, J. Rae, Y. Gao, N. Ariotti, M. Floetenmeyer, O. Kovtun, K.-A. McMahon, N. Chaudhary, R. G. Parton, B. M. Collins

This study shows that Cavin1's intrinsically disordered domains are essential for caveola formation and trafficking through electrostatic interactions and phase separation.

Nature Communications · Feb 10, 2021Peer-reviewedCell Biology