The Serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein Vimentin
2008
Stk33 and Vimentin Interaction Study
publication
Evidence: moderate
Author Information
Author(s): Brauksiepe Bastienne, Mujica Alejandro O, Herrmann Harald, Schmidt Erwin R
Primary Institution: Johannes Gutenberg-University, Mainz, Germany
Hypothesis
Stk33 is involved in the in vivo dynamics of the intermediate filament cytoskeleton by phosphorylating vimentin.
Conclusion
Stk33 phosphorylates vimentin in vitro and interacts with it in vivo.
Supporting Evidence
- Stk33 can specifically phosphorylate the non-α-helical amino-terminal domain of vimentin in vitro.
- Co-immunoprecipitation experiments indicate that Stk33 and vimentin are associated in vivo.
- Stk33 has enzymatic activity as shown by successful phosphorylation of recombinant vimentin proteins.
Takeaway
Stk33 is a protein that helps another protein called vimentin change shape by adding a special tag to it, which is important for how cells are built.
Methodology
The study used in vitro kinase assays, co-immunoprecipitation, and co-sedimentation assays to investigate the interaction between Stk33 and vimentin.
Digital Object Identifier (DOI)
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