Lauren Albrecht
University of California-Irvine, CA·Biochemistry
Every cell must constantly get rid of old, damaged or unneeded proteins to stay healthy. One disposal route, the proteasome, is well understood: proteins marked with a small tag called ubiquitin are recognized and shredded.
- Fields
Biochemistry
Biology
- Topics
lysosome
lysosomal degradation
proteostasis
- Grants
- 1 known grant, through Aug 2029
What they work on
- Identify new proteins that arginine methylation sends to lysosomes for breakdown, and define the short amino acid sequence patterns (peptide motifs) required for their delivery.
- Determine how rapid methyl-driven lysosomal delivery acts as a control switch for core metabolic pathways, including removal of cytosolic enzymes that affects cell growth and proliferation.
- Develop tools based on natural lysosome-targeting signals that let researchers rapidly lower levels of specific proteins in living systems.
- Test whether lysosomes, rather than proteasomes, degrade many short-lived cytosolic proteins, and share findings through a public database of methyl-degraded lysosomal proteins.
More about the research
The other main route, the lysosome, a compartment that digests cell material, is less well understood. Scientists still know little about which proteins are sent to lysosomes and what chemical signals mark them for delivery.
Why it matters
This basic research could explain how cells use lysosomes to control protein lifespans, a core part of keeping cells in balance. A planned public database of methyl-tagged lysosomal proteins could serve researchers who study protein control. New tools for quickly depleting proteins in living systems could make it easier to study what individual proteins do.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Michael James Emanuele
University of North Carolina at Chapel Hill, NC·Biochemistry
Define the wave of protein destruction occurring in G2 and at the G2-to-mitosis transition, determining which proteins are degraded and when, and how the phosphate-adding enzyme PLK1 controls this program, using proteomics and cell-based assays.
Jennifer Kong
University of Washington, WA·Biochemistry
Define the principles by which membrane-tethered E3 ubiquitin ligases, enzymes that tag proteins for destruction, recognize and target cell-surface receptors, mapping their target networks with mass spectrometry and biochemistry.
Y. George Zheng
University of Georgia, GA·Biochemistry
Determine the molecular mechanisms and regulation of protein arginine methyltransferase (PRMT) activity, building on the lab's preliminary results.
The school
University of California-Irvine: 46 labs on PI Pages, $645M a year on research, 524 research doctorates a year.
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