Niels Bradshaw
Brandeis University, MA·Biochemistry
Cells make many of their key decisions by adding phosphate groups to proteins and later removing them. This switch, called reversible phosphorylation, is used by every kingdom of life.
- Fields
Biochemistry
Microbiology & Immunology
Biology
- Topics
protein phosphatases
PPM family
serine/threonine phosphatases
- Grants
- 1 known grant, through Mar 2030
What they work on
- 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.
- Determine how regulatory features that human PPM phosphatases inherited from their bacterial ancestors control the human enzymes, and how these features have been elaborated to meet the needs of human signaling.
- Compare how evolutionarily distinct phosphatase families remove phosphates from the activation loops of MAP kinases, the same highly regulated sites in human signaling cascades, to reveal how phosphatases could be targeted with small molecules.
More about the research
Kinases add the phosphates and phosphatases take them off. Both are often disrupted in disease, which makes them attractive drug targets. Two basic questions about phosphatases remain largely open: how their activity is regulated, and how each one finds the right protein and the right phosphorylated site.
Why it matters
MAP kinase signaling cascades are therapeutic targets in inflammatory diseases and cancer, and PPM phosphatases help control bacterial stress responses and virulence. Showing how these phosphatases are regulated and directed to their targets could suggest new ways to act on them with small-molecule drugs. That knowledge could inform future treatments for cancer, inflammatory disease or bacterial infection.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Elizabeth Libby
Northeastern University, MA·Microbiology & Immunology
Quantitatively dissect how conserved Hanks-type serine/threonine kinase–phosphatase systems in Bacillus subtilis are wired, and how that architecture generates rare single cells with extreme phenotypes such as antibiotic resistance.
Amy Barrios
University of Utah, UT·Biochemistry
Develop fluorogenic peptide substrates, molecules that fluoresce when cut by an enzyme, that are selective for LAR receptor tyrosine phosphatases, using sequences of their known biological targets, and validate them for use in cells.
Jeffrey Hadwiger
Oklahoma State University, OK·Biology
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.
The school
Brandeis University: 5 labs on PI Pages, $107M a year on research, 75 research doctorates a year.
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