Federica Brandizzi
Michigan State University, MI·Biology
Cells build many of their proteins in a compartment called the endoplasmic reticulum (ER), where the proteins must fold into the right shape. Stress, environmental challenges and heavy demand can overwhelm this folding system, a dangerous condition called ER stress.
- Fields
Biology
Plant Science & Agriculture
Biochemistry
- Topics
unfolded protein response
endoplasmic reticulum
ER stress
- Grants
- 1 known grant, last ended Aug 2026
What they work on
- Determine how IRE1, the most conserved UPR sensor and both a protein kinase and an RNA-cutting enzyme, drives protein phosphorylation changes that support growth and relieve ER stress in Arabidopsis.
- Characterize new non-redundant effectors of cell death under unresolvable ER stress, discovered through a whole-plant forward genetic screen in Arabidopsis thaliana.
- Uncover the mechanisms behind the unusual signal transduction pathways of conserved UPR transcription factors, the proteins that switch on stress-response genes, and how they intersect with other pathways.
- Define how the unfolded protein response balances growth, stress resistance and cell-death decisions in a whole multicellular organism, using Arabidopsis genetic and genomic resources.
More about the research
Cells respond with the unfolded protein response (UPR). Sensors in the ER membrane boost the production of folding helpers and clear out misfolded proteins, and if that fails, they trigger cell death. The UPR is essential for growth in multicellular organisms, and its failure is linked to human diabetes, neurodegeneration and cancer. Most UPR research has been done in single-celled organisms or cultured cells, which cannot show how the response works in a whole body.
Why it matters
Defects in protein folding and the UPR are linked to diabetes, neurodegeneration and cancer in humans. Arabidopsis allows whole-body genetic analyses that are not possible in people or mammals. Uncovering how UPR sensors coordinate growth, stress resistance and cell-death decisions could help remove bottlenecks in designing therapies for UPR-associated diseases.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Smriti Sangwan
Northwestern University, IL·Biochemistry·Early-career
Determine how IRE1, an ER stress sensor, physically connects to the protein-making translational machinery, using single-particle cryo-electron microscopy to resolve the 3D structures involved.
Malavika Raman
Tufts University, MA·Biochemistry
Identify how UBXN1 represses translation (protein synthesis at the ribosome), testing whether it binds specific ribosomal proteins in a ubiquitin-dependent way.
Kyaw Aung
Iowa State University, IA·Plant Science & Agriculture·Early-career
Test whether HPCA1, a hydrogen peroxide sensor, functions at plasmodesmata, the channels linking neighboring plant cells, to regulate hydrogen peroxide movement in Arabidopsis thaliana, using genetics and cell biology.
The school
Michigan State University: 28 labs on PI Pages, $932M a year on research, 555 research doctorates a year.
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