Author

A. Karapetsas

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· 3

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Assay:proteomics· 3 Organism:human· 2 Organism:mouse· 1

Frequent Co-Authors

D. R. Alessi· 3 shared R. Gourlay· 3 shared R. S. Nirujogi· 3 shared A. U. Malik· 2 shared M. Wightman· 2 shared S. Knapp· 2 shared S. Mathea· 2 shared A. R. Prescott· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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3 shared papersBiochemistry

D. R. Alessi

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3 papers

Recent·Most cited

PKC isoforms activate LRRK1 kinase by phosphorylating conserved residues (Ser1064, Ser1074 and Thr1075) within the CORB GTPase domain

A. U. Malik, A. Karapetsas, R. S. Nirujogi, D. Chatterjee, T. K. Phung, M. Wightman, R. Gourlay, N. Morrice, S. Mathea, S. Knapp, D. R. Alessi

This study identifies that PKC isoforms activate LRRK1 by phosphorylating specific residues in the CORB GTPase domain, enhancing kinase activity.

bioRxiv · Jun 9, 2022Biochemistry

Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

A. U. Malik, A. Karapetsas, R. S. Nirujogi, S. Mathea, P. Pal, P. Lis, M. Taylor, E. Purlyte, R. Gourlay, M. Dorward, S. Weidlich, R. Toth, N. K. Polinski, S. Knapp, F. Tonelli, D. R. Alessi

This study identifies distinct Rab proteins phosphorylated by LRRK1 and LRRK2, showing they are regulated by different mechanisms and respond differently to inhibitors.

bioRxiv · Nov 25, 2020Biochemistry

Phosphoproteomics reveals that the hVPS34 regulated SGK3 kinase specifically phosphorylates endosomal proteins including Syntaxin-7, Syntaxin-12, RFIP4 and WDR44

N. Malik, R. S. Nirujogi, J. Peltier, T. Macartney, M. Wightman, A. R. Prescott, R. Gourlay, M. Trost, D. R. Alessi, A. Karapetsas

This study identifies novel SGK3 substrates, including endosomal proteins, through phosphoproteomic screens and shows SGK3 specifically phosphorylates these proteins at sites distinct from Akt.

bioRxiv · Aug 20, 2019Biochemistry