Suzanne Pfeffer
Academic Appointments
- Professor, Biochemistry
- Member, Stanford Cancer Institute
- Member, Bio-X
Key Documents
Contact Information
- Academic Offices
Personal Information Email Tel (650) 725-5130
Professional Overview
Administrative Appointments
- Chairman, Stanford University School of Medicine - Biochemistry (2013 - 2015)
- Emma Pfeiffer Merner Professor of Medical Sciences, Stanford University School of Medicine (2012 - present)
- 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)
Honors and Awards
- Fellow, American Academy of Arts and Sciences (2013)
- President, American Society for Biochemistry and Molecular Biology (2010-2012)
- 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 (1978) |
| Ph.D.: | U.C. San Francisco, Biochemistry (1983) |
| Postdoctoral: | U.C. San Francisco, Biochemistry (1984) |
| Postdoctoral: | Stanford University, Biochemistry (1985) |
Graduate & Fellowship Program Affiliations
Internet Links
Scientific Focus
Current Research Interests
During intracellular transport, proteins destined for the plasma membrane, secretory vesicles and lysosomes 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. Current efforts seek to understand how the Golgi complex is formed and how it functions. Although one third of the proteins encoded in the human genome pass through the Golgi, we still do not know how it functions.
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 and NPC1L1 proteins which are essential for cholesterol transport in humans.
Publications
- A nexus for receptor recycling. Nat Cell Biol. 2013; (5): 446-8
- Rab GTPase regulation of membrane identity. Curr Opin Cell Biol. 2013
- Cargo carriers from the Golgi to the cell surface. EMBO J. 2012; (20): 3954-5
- RUTBC2 protein, a Rab9A effector and GTPase-activating protein for Rab36. J Biol Chem. 2012; (27): 22740-8
- Rab GTPase localization and Rab cascades in Golgi transport. Biochem Soc Trans. 2012; (6): 1373-7
- Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase. J Biol Chem. 2012; (50): 42129-37
Help
Trial Administration