Author

P. Varnai

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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Biochemistry· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Balla· 2 shared A. D. Toth· 2 shared A. Inoue· 2 shared G. Turu· 2 shared L. Hunyady· 2 shared S. Prokop· 2 shared A. Acs· 1 shared A. Misak· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersBiochemistry

A. Balla

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

ArreSTick Motif is Responsible for GPCR-beta-Arrestin Binding Stability and Extends Phosphorylation-Dependent beta-arrestin Interactions to Non-Receptor Proteins

A. D. Toth, E. Soltesz-Katona, K. Kis, V. Guti, S. Gilzer, S. Prokop, R. Boros, A. Misak, A. Balla, P. Varnai, L. Turiak, A. Acs, L. Drahos, A. Inoue, L. Hunyady, G. Turu

The paper identifies the arreSTick motif as a key determinant of GPCR-{beta}-arrestin binding stability and shows its presence in non-receptor proteins.

bioRxiv · Aug 4, 2023 · PreprintBiochemistry

Receptor endocytosis orchestrates the spatiotemporal bias of β-arrestin signaling

A. D. Toth, B. Szalai, O. T. Kovacs, D. Garger, S. Prokop, A. Balla, A. Inoue, P. Varnai, G. Turu, L. Hunyady

The study shows that β-arrestin signaling bias is spatiotemporally determined by ligand dissociation rate and G protein activity at endosomes, not receptor conformation.

bioRxiv · Apr 27, 2023Cell Biology

Palmitoylation targets the Calcineurin phosphatase to the Phosphatidylinositol 4-kinase complex at the plasma membrane

I. Ulengin-Talkish, M. A. Parson, M. L. Jenkins, J. Roy, A. Z. Shih, N. St-Denis, G. Gulyas, T. Balla, A.-C. Gingras, P. Varnai, E. Conibear, J. E. Burke, M. S. Cyert

This study identifies palmitoylation as a mechanism that localizes CNA{beta}1 to the plasma membrane and Golgi, enabling its interaction with the PI4KA complex and regulating PI4P production.

bioRxiv · Jul 14, 2021Biochemistry