Malavika Raman
Tufts University, MA·Biochemistry
Cells build many proteins in the endoplasmic reticulum (ER), an internal compartment where membrane and secreted proteins are made and folded. When folding goes wrong, misfolded proteins pile up and harm the cell.
- Fields
Biochemistry
Biology
- Topics
cell biology
biochemistry
endoplasmic reticulum
- Grants
- 1 known grant, through Dec 2027
What they work on
- Identify how UBXN1 represses translation (protein synthesis at the ribosome), testing whether it binds specific ribosomal proteins in a ubiquitin-dependent way.
- Map the pathway through which UBXN1 keeps the unfolded protein response (UPR), the cell's ER stress program, switched off.
- Test whether UBXN1 enables cells to selectively control translation of ER proteins as part of pre-emptive ER quality control, independent of its known partner p97.
More about the research
Such defects underlie diseases ranging from cystic fibrosis to neurodegeneration. Cells have well-known repair systems for this: the unfolded protein response (UPR), a stress program, and ER-associated degradation (ERAD), which destroys bad proteins. Less is known about how cells prevent misfolding in the first place by adjusting protein production at the ribosome, a process called pre-emptive ER quality control.
Why it matters
ER stress and misfolded proteins contribute to many human diseases, including cystic fibrosis and neurodegeneration. By showing how UBXN1 tunes protein production to prevent misfolding before it starts, this work could identify a mechanism that future therapies might activate to protect cells in protein-misfolding 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.
Tom A Rapoport
Harvard University, MA·Biochemistry
Determine how misfolded glycoproteins, proteins carrying sugar chains, are delivered to the Hrd1 complex and moved from the ER interior across the membrane, building on cryo-electron microscopy structures.
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.
The school
Tufts University: 19 labs on PI Pages, $278M a year on research, 144 research doctorates a year.
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