Thesis supervisor: Anita Boratkó
Location of studies (in Hungarian): University of Debrecen, Department of Medical Chemistry Abbreviation of location of studies: DEOVI
Description of the research topic:
Phospho-Ser/Thr-specific protein phosphatases (PP) consist of a catalytic subunit that reversibly binds to further regulatory (R) or interacting partner proteins which control the enzymatic activity. Two major types of Ser/Thr-specific protein phosphatases, PP1 and PP2A, appear to dephosphorylate proteins involved in cytoskeleton/junction/membrane-associated protein interactions, therefore have important role in the regulation cell functions. The enormous number of phospho-Ser/Thr proteins vs. the rather modest variation in phosphatase catalytic subunits implies that the R subunits present in PP1 and PP2A have indeed high impact on the substrate specificity, localization, and regulation of the holoenzyme forms. Therefore, in our study we concentrate on specific regulatory subunits, TIMAP of PP1 and B55/Bα of PP2A, and their newly identified interacting protein partners.
Required language skills: English intermediate level Number of students who can be accepted: 1
Deadline for application: 2024-05-15
2024. IV. 17. ODT ülés Az ODT következő ülésére 2024. június 14-én, pénteken 10.00 órakor kerül sor a Semmelweis Egyetem Szenátusi termében (Bp. Üllői út 26. I. emelet).
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