Rebecca Delventhal
Lake Forest College, IL·Biology
Many of a cell's most important proteins sit in its outer membrane or get shipped outside the cell in small packages. They act as receptors, tethers and signals to other cells, and they are unusually hard to fold into the right shape.
- Fields
Biology
Neuroscience
Genetics
- Topics
ER membrane protein complex
endoplasmic reticulum
membrane protein biogenesis
- Grants
- 1 known grant, through Jul 2027
What they work on
- Determine whether glial EMC4, a subunit of the ER membrane protein complex, is required during development or for maintenance of the adult fly, by timing RNAi knockdown across life stages in Drosophila.
- Identify which specialized nervous system cell types depend on EMC4 for normal survival, locomotion and protein handling, using cell type-specific RNAi knockdown.
- Test whether the shortened survival, locomotor defects and protein aggregation caused by glial EMC4 loss are specific to EMC4 or shared with other subunits of the EMC.
More about the research
That folding happens in the endoplasmic reticulum (ER), a network of internal membranes, with help from specialized protein complexes. One of them is the ER membrane protein complex (EMC), built from 8–10 subunits conserved across species, which is thought to insert membrane proteins, help them fold, and shield them from degradation. Most of what is known about the EMC comes from single-cell systems, so it is unclear whether different cell types or different life stages of an animal depend on it in different ways.
Why it matters
This basic work adds to understanding of how the endoplasmic reticulum builds membrane proteins and whether that process differs between specialized cell types and life stages of a whole animal. Because loss of glial EMC4 shortens life, impairs movement and increases protein clumping in flies, the findings could inform future work on how faulty membrane protein processing in nervous system support cells damages an organism.
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.
Erin Barnhart
Columbia University, NY·Neuroscience
Compare calcium signals in the cytosol and in the endoplasmic reticulum, the neuron's main calcium store, across defined Drosophila motion vision cell types, using simultaneous in vivo imaging in living flies.
Anant Menon
Weill Medical College of Cornell University, NY·Biochemistry
Determine how newly discovered phospholipid scramblases in the outer mitochondrial membrane move lipids, and define their contributions to mitochondrial growth and biogenesis, using a multidisciplinary suite of methods.
The school
Lake Forest College: 2 labs on PI Pages.
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