Jeffrey Hadwiger
Oklahoma State University, OK·Biology
Cells constantly sense signals around them and decide whether to move, grow or change into a new cell type. MAP kinases (MAPKs), enzymes that pass signals along by adding phosphate groups to other proteins, are central to these decisions.
- Fields
Biology
Biochemistry
Genetics
- Topics
MAP kinase
atypical MAPK
Erk2
- Grants
- 1 known grant, last ended Aug 2026
What they work on
- Test whether the atypical MAP kinase Erk2 drives different cell fates in Dictyostelium either by modifying the GATA transcription factor GtaC in different ways or by regulating other transcription factors.
- Map the sites where Erk2 docks on GtaC, a gene-switching protein, using GFP-tagged GtaC. Compare these sites with the docking sites used by other groups of MAP kinases.
- Identify proteins that bind and work with Erk2 in chemotaxis signaling pathways, using co-immunoprecipitation, mass spectrometry and genetic analysis.
- Identify the unconventional upstream kinase or other proteins that directly switch on Erk2, since Erk2 does not activate itself.
More about the research
A little-studied group, the atypical MAPKs, exists only in organisms whose cells can move. In mammals this group includes MAPK15, also called Erk8. Little is known about what switches these kinases on or what they control. The amoeba Dictyostelium is the one organism where the outside signals that activate them are known. Dictyostelium is a model for chemotaxis, the movement of cells toward a chemical signal, and for development.
Why it matters
This is basic research on how cells read signals to move and choose their fate. Atypical MAPKs like MAPK15/Erk8 are found in mammals but poorly understood. Mechanisms uncovered in Dictyostelium could guide studies of these kinases in other organisms, including mammals.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Niels Bradshaw
Brandeis University, MA·Biochemistry
Uncover general principles of how PPM serine/threonine phosphatases are regulated and directed to the right substrate, using bacterial phosphatases that control the general stress response, a survival pathway linked to virulence.
Peter Lundquist
Michigan State University, MI·Plant Science & Agriculture·Early-career
Measure the protein kinase activity of each of the six plastoglobule ABC1 kinases (ABC1Ks), enzymes that add phosphate tags to proteins, using in vitro kinase assays with ABC1Ks expressed in a separate host organism.
Douglas N Robinson
Johns Hopkins University, MD·Biophysics
Test SpringSaLaD computer-model predictions about how Contractility Kits, premade bundles of myosin II, cortexillin I and IQGAP proteins, form in Dictyostelium amoebae, using measured cellular concentrations and binding strengths.
The school
Oklahoma State University: 15 labs on PI Pages, $254M a year on research, 238 research doctorates a year.
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