Suzanne Pfeffer

Last updated
Suzanne Pfeffer
Suzanne Pfeffer 2010 (cropped).jpg
Pfeffer in 2010
Born
Suzanne Ruth Pfeffer
Alma mater University of California, Berkeley (BS)
University of California, San Francisco (PhD)
Scientific career
Fields Parkinson's disease [1]
Institutions Stanford University
Thesis The role of coated vesicles in intracellular transport  (1983)
Website profiles.stanford.edu/suzanne-pfeffer OOjs UI icon edit-ltr-progressive.svg

Suzanne Ruth Pfeffer is an American neuroscientist who is a professor at Stanford University. [2] Her research investigates the molecular mechanisms that cause receptors to be transported between membrane compartments in cells, and she is an expert in Rab GTPases [3] [4] [5] and the molecular basis of inherited Parkinson's disease. [1] She is a Fellow of the American Association for the Advancement of Science, American Academy of Arts and Sciences and the American Society for Cell Biology. [6]

Contents

Early life and education

Pfeffer has said that she became interested in human physiology as a child. She was an undergraduate student at the University of California, Berkeley, where she became interested in biochemistry. [7] She worked with Michael Chamberlin on binding of Escherichia coli polymerase to T7 DNA polymerase. [8] She moved to the University of California, San Francisco for her graduate studies, where she worked with Regis B. Kelly on synaptic vessels. [7] Her doctoral research investigated the role of coated vesicles in intracellular transport. [9]

Research and career

After her PhD, she moved to Stanford University as a Hay Whitney postdoctoral fellow, where she worked with James Rothman on Golgi transport. [7] [10]

Pfeffer set up her own research program at Stanford University, where she was the first woman to be appointed to the department of biochemistry. [7] Her research investigates the fundamental mechanisms of membrane trafficking. [7] [11]

Selected publications

Awards and honors

Related Research Articles

<span class="mw-page-title-main">Endocytosis</span> Cellular process

Endocytosis is a cellular process in which substances are brought into the cell. The material to be internalized is surrounded by an area of cell membrane, which then buds off inside the cell to form a vesicle containing the ingested materials. Endocytosis includes pinocytosis and phagocytosis. It is a form of active transport.

<span class="mw-page-title-main">Golgi apparatus</span> Cell organelle that packages proteins for export

The Golgi apparatus, also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. Part of the endomembrane system in the cytoplasm, it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus.

<span class="mw-page-title-main">Vesicle (biology and chemistry)</span> Any small, fluid-filled, spherical organelle enclosed by a membrane

In cell biology, a vesicle is a structure within or outside a cell, consisting of liquid or cytoplasm enclosed by a lipid bilayer. Vesicles form naturally during the processes of secretion (exocytosis), uptake (endocytosis), and the transport of materials within the plasma membrane. Alternatively, they may be prepared artificially, in which case they are called liposomes. If there is only one phospholipid bilayer, the vesicles are called unilamellar liposomes; otherwise they are called multilamellar liposomes. The membrane enclosing the vesicle is also a lamellar phase, similar to that of the plasma membrane, and intracellular vesicles can fuse with the plasma membrane to release their contents outside the cell. Vesicles can also fuse with other organelles within the cell. A vesicle released from the cell is known as an extracellular vesicle.

<span class="mw-page-title-main">Endosome</span> Vacuole to which materials ingested by endocytosis are delivered

Endosomes are a collection of intracellular sorting organelles in eukaryotic cells. They are parts of the endocytic membrane transport pathway originating from the trans Golgi network. Molecules or ligands internalized from the plasma membrane can follow this pathway all the way to lysosomes for degradation or can be recycled back to the cell membrane in the endocytic cycle. Molecules are also transported to endosomes from the trans Golgi network and either continue to lysosomes or recycle back to the Golgi apparatus.

The Rab family of proteins is a member of the Ras superfamily of small G proteins. Approximately 70 types of Rabs have now been identified in humans. Rab proteins generally possess a GTPase fold, which consists of a six-stranded beta sheet which is flanked by five alpha helices. Rab GTPases regulate many steps of membrane trafficking, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled. Surface protein recycling returns proteins to the surface whose function involves carrying another protein or substance inside the cell, such as the transferrin receptor, or serves as a means of regulating the number of a certain type of protein molecules on the surface.

<span class="mw-page-title-main">RAB5A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-5A is a protein that in humans is encoded by the RAB5A gene.

<span class="mw-page-title-main">RAB7A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-7a is a protein that in humans is encoded by the RAB7A gene.

<span class="mw-page-title-main">RAB8A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-8A is a protein that in humans is encoded by the RAB8A gene.

<span class="mw-page-title-main">RAB9A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-9A is a protein that in humans is encoded by the RAB9A gene.

<span class="mw-page-title-main">RAB11B</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-11B is a protein that in humans is encoded by the RAB11B gene. Rab11b is reported as most abundantly expressed in brain, heart and testes.

<span class="mw-page-title-main">RABEPK</span> Protein-coding gene in the species Homo sapiens

Rab9 effector protein with Kelch motifs also known as p40 is a protein that in humans is encoded by the RABEPK gene.

<span class="mw-page-title-main">Jennifer Lippincott-Schwartz</span> American biologist

Jennifer Lippincott-Schwartz is a Senior Group Leader at Howard Hughes Medical Institute's Janelia Research Campus and a founding member of the Neuronal Cell Biology Program at Janelia. Previously, she was the Chief of the Section on Organelle Biology in the Cell Biology and Metabolism Program, in the Division of Intramural Research in the Eunice Kennedy Shriver National Institute of Child Health and Human Development at the National Institutes of Health from 1993 to 2016. Lippincott-Schwartz received her PhD from Johns Hopkins University, and performed post-doctoral training with Richard Klausner at the NICHD, NIH in Bethesda, Maryland.

<span class="mw-page-title-main">STX10</span> Protein-coding gene in the species Homo sapiens

Syntaxin-10 (STX10) is a SNARE protein that is encoded by the STX10 gene. This protein is found in most vertebrates but is noticeably absent from mice. As with other SNARE proteins, STX10 facilitates vesicle fusion and thus is important for intracellular trafficking of proteins and other cellular components. More specifically, STX10 has been implicated in endosome to Golgi trafficking of the mannose 6-phosphate receptor and glucose transporter type 4.

<span class="mw-page-title-main">Anne Spang</span> German biochemist, cell biologist, and professor

Anne Spang is a German Biochemist/Cell Biologist and Professor at the Biozentrum University of Basel, Switzerland.

Rab GTPases are molecular switches that regulate membrane traffic. They are active in their GTP-bound form and inactive when bound to GDP. The GTPase YPT1, and its mammalian homologue Rab1, regulate membrane-tethering events on three different pathways: autophagy, ER-Golgi, and intra-Golgi traffic. In the yeast Saccharomyces cerevisiae, many of the ATG proteins needed for macroautophagy are shared with the biosynthetic cytoplasm to the vacuole-targeting (CVT) pathway that transports certain hydrolases into the vacuole. Both pathways require YPT1; however, only the macroautophagy pathway is conserved in higher eukaryotes. In the macroautophagy pathway, Rab1 mediates the recruitment of Atg1 to the PAS. Rab1 regulates macroautophagy by recruiting its effector, Atg1, to the PAS to tether Atg9 vesicles to each other or to other membranes.

<span class="mw-page-title-main">Sandra Schmid</span> Canadian biologist

Sandra Louise Schmid is the first Chief Scientific Officer of the Chan Zuckerberg Biohub. She is a Canadian cell biologist by training; prior to her move to CZ Biohub, she was Professor and Chair of the Cell Biology Department at the University of Texas Southwestern Medical Center. Throughout her academic career, she has authored over 105 publications on the molecular mechanism and regulation of clathrin-mediated endocytosis and the structure and function of the GTPase dynamin and mechanisms governing membrane fission. She was the first to identify dynamin's key role in endocytosis. She is a co-founder of the journal Traffic and has been the Editor-in-Chief of Molecular Biology of the Cell, and the President of the American Society for Cell Biology.

<span class="mw-page-title-main">Anne Ridley</span> Professor of Cell Biology

Anne Jacqueline Ridley is professor of Cell Biology and Head of School for Cellular and Molecular Medicine at the University of Bristol. She was previously a professor at King's College London.

<span class="mw-page-title-main">Yukiko Goda</span> Japanese molecular biologist and academic

Yukiko Goda is a Japanese molecular biologist who is a professor and group leader at the Okinawa Institute of Science and Technology. Her research considers neural communication through synapses. She was elected a Member of the European Molecular Biology Organization in 2023.

<span class="mw-page-title-main">Gia Voeltz</span> American cell biologist

Gia Voeltz is an American cell biologist. She is a professor of Molecular, Cellular and Developmental Biology at the University of Colorado Boulder and a Howard Hughes Medical Institute Investigator. She is known for her research identifying the factors and unraveling the mechanisms that determine the structure and dynamics of the largest organelle in the cell: the endoplasmic reticulum. Her lab has produced paradigm shifting studies on organelle membrane contact sites that have revealed that most cytoplasmic organelles are not isolated entities but are instead physically tethered to an interconnected ER membrane network.

<span class="mw-page-title-main">RAB4B</span>

Ras-related protein Rab-4B is a protein that in humans is encoded by the RAB4B gene.

References

  1. 1 2 Suzanne Pfeffer publications indexed by Google Scholar OOjs UI icon edit-ltr-progressive.svg
  2. Suzanne Pfeffer publications from Europe PubMed Central
  3. 1 2 Suzanne R. Pfeffer; James E. Rothman (1 January 1987). "Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi". Annual Review of Biochemistry . 56: 829–852. doi:10.1146/ANNUREV.BI.56.070187.004145. ISSN   0066-4154. PMID   3304148. Wikidata   Q39664981.
  4. 1 2 D Lombardi; Thierry Soldati; M A Riederer; Y Goda; M Zerial; S R Pfeffer (1 February 1993). "Rab9 functions in transport between late endosomes and the trans Golgi network". The EMBO Journal . 12 (2): 677–682. doi:10.1002/J.1460-2075.1993.TB05701.X. ISSN   0261-4189. PMC   413253 . PMID   8440258. Wikidata   Q28609814.
  5. 1 2 Pfeffer SR (December 2001). "Rab GTPases: specifying and deciphering organelle identity and function". Trends in Cell Biology . 11 (12): 487–91. doi:10.1016/S0962-8924(01)02147-X. ISSN   0962-8924. PMID   11719054. Wikidata   Q29620750.
  6. profiles.stanford.edu/suzanne-pfeffer OOjs UI icon edit-ltr-progressive.svg
  7. 1 2 3 4 5 Sedwick, Caitlin (2009-04-06). "Suzanne Pfeffer: Sorting through membrane trafficking". Journal of Cell Biology. 185 (1): 4–5. doi:10.1083/jcb.1851pi. ISSN   1540-8140. PMC   2700508 . PMID   19349576.
  8. Pfeffer, S. R.; Stahl, S. J.; Chamberlin, M. J. (1977-08-10). "Binding of Escherichia coli RNA polymerase to T7 DNA. Displacement of holoenzyme from promoter complexes by heparin". The Journal of Biological Chemistry. 252 (15): 5403–5407. ISSN   0021-9258. PMID   328501.
  9. Pfeffer, Suzanne Ruth. The role of coated vesicles in intracellular transport. escholarship.org (PhD thesis). OCLC   1020060429. ProQuest   303125660.
  10. "Suzanne R. Pfeffer, PhD | Parkinson's Disease". michaeljfox.org. Retrieved 2023-07-23.
  11. Pfeffer, Suzanne; Aivazian, Dikran (2004). "Targeting Rab GTPases to distinct membrane compartments". Nature Reviews Molecular Cell Biology . 5: 886–896.
  12. "Inside AAAS". www.science.org. Science. 2023-07-23. Retrieved 2024-05-28.
  13. "ASCB Presidents". ascb.org. Retrieved 2023-07-23.
  14. "Past presidents". asbmb.org. Retrieved 2023-07-23.
  15. "Suzanne Pfeffer". amacad.org. American Academy of Arts & Sciences. 2023-07-23. Retrieved 2023-07-23.
  16. "Suzanne Pfeffer - ASCB". ascb.org. The American Society for Cell Biology. 2024-05-28. Retrieved 2024-05-28.
  17. "National Academy of Sciences Elects Members and International Members". www.nasonline.org. 30 April 2024. Retrieved 12 May 2024.