Smriti Sangwan
Northwestern University, IL·Biochemistry·Early-career
Cells must fold their proteins correctly, and they must quickly deal with proteins that fold wrongly. Much of this work happens in the endoplasmic reticulum (ER), the cell compartment where most membrane and secreted proteins are folded and finished.
- Fields
Biochemistry
Biophysics
Biology
- Topics
unfolded protein response
inositol requiring enzyme 1
endoplasmic reticulum
- Grants
- 1 known grant, through Mar 2028
What they work on
- 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.
- Identify which messenger RNAs have their translation fine-tuned by IRE1 at the ER, using sequencing-based functional genomics methods.
- Ask whether other unfolded protein response sensors besides IRE1 also regulate translation, building a molecular model of how cells avoid overloading the ER's protein-folding machinery.
More about the research
When the ER fails, misfolded proteins build up and cause "ER stress." ER dysfunction is linked to about a dozen diseases, including diabetes, neurodegenerative diseases and cancer. Cells respond with the unfolded protein response (UPR), a set of sensors that detect folding trouble and adjust the cell's activity.
Why it matters
ER stress and unresolved protein aggregation are tied to diabetes, neurodegenerative diseases and cancer. A detailed molecular account of how IRE1 controls protein production at the ER would add basic understanding of cellular protein quality control. It could eventually inform efforts to target the unfolded protein response in these diseases.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Federica Brandizzi
Michigan State University, MI·Biology
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.
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.
Qinglian Liu
Virginia Commonwealth University, VA·Biochemistry
Determine the in vivo role of Hsp110 holdase activity (keeping unfolded proteins from clumping) in protein folding, using the selective inhibitor 2H and the genetics of the yeast Saccharomyces cerevisiae.
The school
Northwestern University: 71 labs on PI Pages, $1.3B a year on research, 536 research doctorates a year.
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