The Lau Lab is a research group in the Department of Medicine at the University of Colorado School of Medicine. We study the regulation and function of protein turnover, homeostasis, and secretion using proteomics and bioinformatics methods.
Current Position: PharmD Student, CU Anschutz
Current Position: PhD Student, U of Michigan
Current Position: Data Scientist, Fred Hutch
Current Position: Senior LSRP, CU Anschutz
Current Position: PhD Student, CU Anschutz BioE
Current Position: Med. Lab Manager, CU Anschutz
Current Position: Student, CU Boulder
Current Position: PhD Student, CU Anschutz IPHY
Current Position: Senior LSRP, CU Anschutz
Current Position: PhD Student, CU Anschutz CSD
Current Position: Student, CU Denver
Current Position: Stem Cell Technician, ClinImm…
Current Position: Student, CU Anschutz
The function of a protein is determined not only by its abundance, but also by its synthesis and degradation rate, post-translational modifications, and subcellular localization. Our lab studies how these dynamic parameters influence cellular homeostasis, aging, and disease on a proteome scale, using a combination of proteomics and bioinformatics approaches. Several areas of current focus include:
What is the role of protein turnover and homeostasis during cell fate transitions?
Our lab develops analytical and computational methods that can measure the individual turnover rates and half-life of thousands of protein species in complex systems. These techniques have been used to reveal changes in protein synthesis and degradation in animal models and discover new disease signatures. A current focus is to understand the regulation and function of protein quality control and proteolysis during cellular differentiation, stress, and senescence in iPSC systems.How do cells in the body communicate through secreted RNAs and proteins?
In recent work, we have mapped secreted non-coding RNAs from multiple cell types derived from human induced pluripotent stem cells (hiPSCs) (cardiomyocytes, endothelial cells, fibroblasts) that may function in intercellular communications and that may be harnessed as a quantitative metric to assess the differentiation status and purity of hiPSC-derived cardiac cells. In ongoing work, we are leveraging this approach to model the longitudinal changes in cellular communication networks under stress and disease using a combination of computational modeling and proteomics strategies.How does subcellular localization affect protein synthesis and degradation?
Our lab has developed a method to measure the turnover rates of proteins in different subcellular compartments which we call SPLAT (Simultaneous Proteome Localization and Turnover). In ongoing work, we are using this method to understand how the spatial organization of protein synthesis and degradation is regulated in response to ER stress, proteasome inhibition, and other cellular perturbations.Work in the laboratory is supported by funding from NIGMS, NHLBI, NHGRI, the University of Colorado Translational Research Scholars Program, and the University of Colorado Consortium for Fibrosis Research & Translation. We have funded positions open for undergraduates, post-bacs, graduate students, and post-doctoral fellows! Come work with us if you are interested in protein regulations and wish to hone your research skills in a friendly and supportive environment.
A new project from our lab explores "simultaneous proteome localization and turnover" analysis.
When does mRNA level not predict protein level? A new paper from our lab revisited the question of how well mRNA levels reflect protein variances across different tumors and normal tissues using CPTAC data.
Using mass spectrometry, stable isotope labeling, and kinetic modeling to determine protein half-life in vivo.
We are interested in applying proteomics and bioinformatics methods to discover secreted proteins and long-range endocrine signals from different cells and tissues.