Richard Anderson, PhD
Position title: Professor, Dean's Office, Basic Sciences
Room 6159 WIMR1
1111 Highland Ave
Madison, WI 53713
- Lab Website
- Anderson Lab
Cell Signaling from Receptor to the Nucleus; Systems Biology; Cancer Biology
The goals of the Anderson lab’s research are to understand the biological roles of cell signaling and the underlying mechanisms by which receptors, cell stresses and second messengers modulate specific cellular processes. The research is currently focused in two broad general areas.
Signaling pathways that control cell proliferation, autophagy and cancer. This research is focused on signaling pathways that regulate multiple cellular processes including cell morphogenesis, migration, growth and differentiation. A major focus is on phosphoinositide lipid messengers. This is within the focus is on the role of growth factor and integrin receptor signaling pathways that controls the morphogenesis, proliferation, migration and cell death with an emphasis on downstream signaling and membrane trafficking of receptors. These pathways are fundamental to most cancers and this work is translated to several cancers by collaborations with other groups.
Signaling to the Nucleus and gene expression. We have discovered and pioneered the investigation of novel nuclear signaling pathways that ultimately control gene expression. Within the nucleus that there are phosphoinositide lipid messengers pathways at nuclear compartments that are separate from known membrane structures. We have shown that nuclear phosphoinositide pathways control the 3’-processing of mRNAs, activation of select transcriptional pathways, and modulation of pathways that posttranslationally modify nuclear proteins. Most recently we have discovered that both wild type p53 (a tumor suppressor) and mutant p53 (an oncogene) are control by phosphoinositide lipid messengers and this regulates all aspects of p53 function. These nuclear pathways are fundamental to all aspects of cellular function and are important in many human diseases.
The laboratory uses cutting edge techniques including: 1) cell culture, 2) videomicroscopy of cells and molecular dynamics of proteins within living cells, 3) screening for potential drugs, 4) 3-D structure-function analysis, 5) expression of genes with functionally targeted mutations, 6) microarray analysis of gene expression, 7) knock out techniques, 8) molecular genetic analysis of gene expression, and 9) molecular biological approaches to analyze for analysis of signal transduction mechanisms.
Honors & Awards
- 2005 – Kellett Mid-Career Award
- Sigma Xi Graduate Research Award
- NIH Postdoctoral Fellowship
- American Cancer Society Postdoctoral Fellowship
- Bacaner Basic Science Award
- Schill, N.J., Hedman, A.C., Choi, S. and Anderson, R.A. (2014) Isoform 5 of PIPKIγ regulates the endosomal trafficking and degradation of E-cadherin. J. Cell Science. 127, 2189-2203, PMID: 24610942, PMCID: PMC4021470 Emphasized in the JCS Snapshot
- Tan, X., Thapa, N., Sun, Y. & Anderson, R.A. (2015) A kinase-independent role for EGF receptor in autophagy initiation. Cell 160, 145-160. PMID: 25594178, PMCID: PMC4297316. News release UW, Emphasized in Science Comments, Oncology-central, Science Daily, Cancer Discovery – News in Brief, “Study Illuminates How Cancers Evade EGFR Inhibitors”
- Tan X, Sun Y, Thapa N, Liao Y, Hedman AC, Anderson RA. (2015) LAPTM4B is a PtdIns(4,5)P2 effector that regulates EGFR signaling, lysosomal sorting, and degradation. The EMBO journal. PMID: 25588945, “PMCID: PMC4331002
- Choi, S., Thapa, N., Tan, X., Hedman, A.C. & Anderson, R.A. (2015) PIP kinases define PI4,5P signaling specificity by association with effectors. Biochimica et biophysica acta 1851, 711-723. PMID: 25617736, PMCID: PMC4380618
- Thapa, N., Choi, S., Tan, X., Wise, T. & Anderson, R.A. (2015) Phosphatidylinositol Phosphate 5-Kinase Igamma and PI3K/Akt Signaling Couple to Promote Oncogenic Growth. In press, J. Biol. Chem.
- Choi, S., Hedman, A.C., Thapa, N., Sacks, D., and Anderson, R.A. (2015) Agonist-stimulated PI3,4,5P3 generation by scaffolded phosphoinositide kinases. In revision, Nature.