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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Rab-GTPase binding effector protein 2 (RABEP2) is a primed substrate for Glycogen Synthase kinase-3 (GSK3).

Lisa Logie1, Lidy Van Aalten1, Axel Knebel2

  • 1Division of Molecular and Clinical Medicine, University of Dundee, Dundee, UK.

Scientific Reports
|December 17, 2017
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Glycogen synthase kinase-3 (GSK3) phosphorylates Rab-GTPase binding effector protein 2 (RABEP2) at Ser200. This identifies RABEP2 as a novel GSK3 substrate and potential biomarker for GSK3 activity.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Glycogen synthase kinase-3 (GSK3) is a key regulator of numerous physiological processes via substrate phosphorylation.
  • GSK3 inhibitors are explored for therapeutic use, but GSK3's essential cellular roles pose challenges.
  • Identifying specific GSK3 substrates is crucial for targeted disease therapies.

Purpose of the Study:

  • To identify novel, kinetically favorable substrates of GSK3.
  • To investigate the phosphorylation of Rab-GTPase binding effector protein 2 (RABEP2) by GSK3.

Main Methods:

  • Performed a GSK3 substrate screen in heart tissue.
  • Analyzed GSK3 phosphorylation of RABEP2 at Ser200 and Ser204.
  • Investigated RABEP2 localization and function in cells, including co-localization with Rab5 and effects on endosomal recycling.

Main Results:

  • Identified Rab-GTPase binding effector protein 2 (RABEP2) as a novel GSK3 substrate.
  • Confirmed GSK3 phosphorylates RABEP2 at Ser200, a process enhanced by prior Ser204 phosphorylation.
  • Observed Ser200 phosphorylation reduction upon GSK3 inhibition in cells.
  • Found no co-localization of RABEP2 with Rab5 or impact on endosomal recycling.

Conclusions:

  • RABEP2 is a novel primed substrate of GSK3.
  • RABEP2 may serve as a biomarker for GSK3 activity.
  • Further research is needed to elucidate the functional consequences of RABEP2 phosphorylation by GSK3.