Suzanne Pfeffer
Academic Appointments
- Professor, Biochemistry
- Member, Bio-X
- Member, Cancer Center
Contact Information
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Academic Offices
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Professional Snapshot
Administrative Appointments
- Professor, Stanford University School of Medicine-Biochemistry (1998 - present)
- Chair, Stanford University School of Medicine - Biochemistry (1998 - 2006)
- Associate Chairman, Stanford University School of Medicine-Biochemistry (1997 - 1998)
- Associate Professor, Stanford University School of Medicine - Biochemistry (1992 - 1998)
- Assistant Professor, Stanford University School of Medicine-Biochemistry (1986 - 1992)
Honors and Awards
- President-elect, American Society for Biochemistry and Molecular Biology (2009-2010)
- President, American Society for Cell Biology (2003)
- Merit Award, National Institute of Diabetes and Digestive and Kidney Disorders (1999-2009)
- Fellow, American Association for the Advancement of Science (1992)
- Presidential Young Investigator Award, National Science Foundation (1988-1993)
Professional Education
| A.B.: | U.C. Berkeley, Biochemistry (1977) |
| Ph.D.: | U.C. San Francisco, Biochemistry (1983) |
| Postdoctoral: | U.C. San Francisco, Biochemistry (1984) |
| Postdoctoral: | Stanford University, Biochemistry (1985) |
Postdoctoral Advisees
Graduate & Fellowship Program Affiliations
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Scientific Focus
Research Interests
During intracellular transport, proteins destined for the plasma membrane, secretory vesicles and prelysosomes must be sorted from one another within the Golgi complex and sent to their appropriate addresses. The long term goal of our research is to elucidate the molecular mechanisms by which proteins are targeted to specific and distinct compartments. We would like to understand how transport vesicles select their contents, bud off from an organelle, translocate through the cytoplasm to recognize their target, and then fuse with their target to deliver specific cargo molecules. We study a specific intracellular transport step: transport of mannose 6-phosphate receptors from late endosomes to the trans Golgi network. We discovered a Ras-like GTPase, Rab9, that is required for this process, as well as a protein named TIP47 that works with Rab9 to help package mannose 6-phosphate receptors into transport vesicles. Also required are a Golgi tether that is needed for vesicle docking (GCC185), and an unusual Rho GTPase family member that is actually an ATPase and may uncoat vesicles as they arrive at the Golgi. Current efforts seek to understand how these proteins work together to drive a specific transport event.
A molecular understanding of membrane traffic has broad implications for our understanding of growth control in cancer, receptor trafficking errors in heart disease, regulation of insulin secretion in diabetes and synaptic vesicle biogenesis and transport in neurological disorders. We also study the NPC1 protein which is essential for cholesterol regulation in humans and when mutated, leads to Niemann Pick Type C disease.
Publications
- Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi. Mol Biol Cell. 2009; (1): 209-17
- RhoBTB3: a Rho GTPase-family ATPase required for endosome to Golgi transport. Cell. 2009; (5): 938-48
- Multiple routes of protein transport from endosomes to the trans Golgi network. FEBS Lett. 2009
- Defining the boundaries: Rab GEFs and GAPs. Proc Natl Acad Sci U S A. 2009; (34): 14185-6
- WHAMMing into the Golgi. Dev Cell. 2008; (2): 171-2
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