Research Topics
Species | S PfefferSummaryAffiliation: Stanford University Country: USA Publications
Research Grants
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Detail Information
Publications
WHAMMing into the GolgiGarret L Hayes
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Dev Cell 15:171-2. 2008..WHAMM's membrane localization at the entry face of the Golgi complex is novel for an actin nucleation-promoting factor, and highlights the importance of the cytoskeleton in organizing the secretory pathway...- Rab GTPase localization and Rab cascades in Golgi transportSuzanne R Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Biochem Soc Trans 40:1373-7. 2012..Finally, I describe how Rab cascades may establish the distinct compartments of the Golgi complex to permit ordered processing, sorting and secretion of secretory cargoes... 
Cargo carriers from the Golgi to the cell surfaceSuzanne R Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA
EMBO J 31:3954-5. 2012..CARTS appear to be basolateral membrane-directed carriers that use myosin for their motility but not for their formation...- How the Golgi works: a cisternal progenitor modelSuzanne R Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Proc Natl Acad Sci U S A 107:19614-8. 2010.... - Unconventional secretion by autophagosome exocytosisSuzanne R Pfeffer
Department of Biochemistry, School of Medicine, Stanford University, Stanford, CA 94305, USA
J Cell Biol 188:451-2. 2010..Medium-chain acyl CoAs are also required and may be important for substrate routing to this pathway... 
Two Rabs for exosome releaseSuzanne R Pfeffer
Suzanne Pfeffer is at the Department of Biochemistry, Stanford University School of Medicine, 279 Campus Drive B400, Stanford, CA 94305 5307, USA
Nat Cell Biol 12:3-4. 2010..Rab27A and Rab27B GTPases and two of their cognate effector proteins seem to be needed to drive the physiologically important exosome-release process in certain cell types...- Multiple routes of protein transport from endosomes to the trans Golgi networkSuzanne R Pfeffer
Department of Biochemistry, 279 Campus Drive B400, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
FEBS Lett 583:3811-6. 2009..The identification of distinct molecular requirements for each of these pathways makes it clear that mammalian cells have evolved more complex targeting mechanisms and routes than previously anticipated... - Unsolved mysteries in membrane trafficSuzanne R Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
Annu Rev Biochem 76:629-45. 2007..But much remains to be learned. This review highlights underlying themes in membrane traffic to help us refocus and solve many remaining and newly emerging issues that are fundamental to mammalian cell biology and human physiology... - A model for Rab GTPase localizationS Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Biochem Soc Trans 33:627-30. 2005..Our data suggest that these complex interactions are important for the cellular localization of Rab proteins at steady state... - Structural clues to Rab GTPase functional diversitySuzanne R Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
J Biol Chem 280:15485-8. 2005..This review will highlight what we have learned from crystallographic analysis of this important protein family... - Targeting Rab GTPases to distinct membrane compartmentsSuzanne Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
Nat Rev Mol Cell Biol 5:886-96. 2004..The further discovery of an integral membrane protein that can dissociate prenylated Rab proteins from GDP-dissociation inhibitor gives new insights into the mechanisms of Rab localization... - Membrane domains in the secretory and endocytic pathwaysSuzanne Pfeffer
Department of Biochemistry, Stanford University, Stanford, CA 94305, USA
Cell 112:507-17. 2003..Thus, functionally distinct specializations of a given organelle are physically segregated to a greater extent than previously believed... - Cholesterol accumulation sequesters Rab9 and disrupts late endosome function in NPC1-deficient cellsIan G Ganley
Department of Biochemistry, Stanford University School of Medicine, 279 Campus Drive, Stanford, CA 94305 5307, USA
J Biol Chem 281:17890-9. 2006..We conclude that cholesterol contributes directly to the sequestration of Rab9 on Niemann-Pick type C cell membranes, which in turn, disrupts mannose 6-phosphate receptor trafficking... - Vesicle tethering factors unitedS Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA
Mol Cell 8:729-30. 2001.... 
Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cellsPierre Barbero
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA
J Cell Biol 156:511-8. 2002..Our data suggest that Rab9 remains vesicle associated until docking with the Golgi complex and is rapidly removed concomitant with or just after membrane fusion...- A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cellsIan G Ganley
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA
J Cell Biol 180:159-72. 2008..Importantly, our data provide a clear molecular distinction between the transport of MPRs and TGN46 to the trans-Golgi... - Vesicle traffic: get your coat!F Schimmöller
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
Curr Biol 7:R235-7. 1997.... - Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185Alondra Schweizer Burguete
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA
Cell 132:286-98. 2008.... - Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-GolgiGarret L Hayes
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA
Mol Biol Cell 20:209-17. 2009..Golgi-Rab binding sites may permit GCC185 to contribute to stacking and lateral interactions of Golgi cisternae as well as help it function as a vesicle tether... - TBC1D20 is a Rab1 GTPase-activating protein that mediates hepatitis C virus replicationElla H Sklan
Department of Medicine, Division of Gastroenterology and Hepatology, Stanford University School of Medicine, Palo Alto, CA 94305 5187, USA
J Biol Chem 282:36354-61. 2007..These results highlight a novel mechanism by which viruses can hijack host cell machinery and suggest an attractive model whereby the NS5A-TBC1D20 interaction may promote viral membrane-associated RNA replication... - Yip3 catalyses the dissociation of endosomal Rab-GDI complexesUlf Sivars
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
Nature 425:856-9. 2003..We propose that the conserved Yip proteins serve as GDI-displacement factors for the targeting of Rab GTPases in eukaryotic cells... - Clues to neuro-degeneration in Niemann-Pick type C disease from global gene expression profilingJonathan V Reddy
Department of Biochemistry, Stanford University School of Medicine, California, United States of America
PLoS ONE 1:e19. 2006..The majority of NPC cases are due to mutations in the NPC1 gene. The precise function of this gene is not yet known... - Identification of residues in TIP47 essential for Rab9 bindingJohn Hanna
Department of Biochemistry, Stanford University School of Medicine, 279 Campus Drive, Stanford, CA 94305 5307, USA
Proc Natl Acad Sci U S A 99:7450-4. 2002..These experiments reveal distinct binding domains for the Rab9 GTPase and MPR cytoplasmic domains in the cargo selection protein TIP47... - A functional role for the GCC185 golgin in mannose 6-phosphate receptor recyclingJonathan V Reddy
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Mol Biol Cell 17:4353-63. 2006..These data assign a specific pathway to an interesting, TGN-localized protein and suggest that GCC185 may participate in the docking of late endosome-derived, Rab9-bearing transport vesicles at the TGN... - Team effort by TRAPP forces a nucleotide fumbleRyan M Nottingham
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Cell 133:1141-3. 2008..Cai et al. (2008) now present structural and biochemical analyses of yeast TRAPPI in a complex with Ypt1p revealing a unique mechanism by which TRAPPI catalyzes guanine nucleotide exchange... - RhoBTB3: a Rho GTPase-family ATPase required for endosome to Golgi transportEric J Espinosa
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Cell 137:938-48. 2009..Because RhoBTB3 interacts with TIP47 on membranes, we propose that it may function to release this cargo selection protein from vesicles to permit their efficient docking and fusion at the Golgi... - Self-assembly is important for TIP47 function in mannose 6-phosphate receptor transportPaul M Sincock
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Traffic 4:18-25. 2003..However, oligomerization is required for TIP47 stimulation of mannose 6-phosphate receptor transport from endosomes to the trans-Golgi in vivo... - Association of beta-1,3-N-acetylglucosaminyltransferase 1 and beta-1,4-galactosyltransferase 1, trans-Golgi enzymes involved in coupled poly-N-acetyllactosamine synthesisPeter L Lee
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA
Glycobiology 19:655-64. 2009..These results demonstrate that B3GNT1 and B4GALT1 physically associate in vitro and in cultured cells, providing insight into possible mechanisms for regulation of polyLacNAc production... - In vitro selection and prediction of TIP47 protein-interaction interfacesAlondra Schweizer Burguete
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
Nat Methods 1:55-60. 2004..These methods were validated in comparison with the protein's crystal structure, and provide a powerful means to predict protein-protein interaction interfaces...
Research Grants
- INTRACELLULAR TRANSPORT--THE MANNOSE-PHOSPHATE RECEPTORSuzanne Pfeffer; Fiscal Year: 2007..These studies have important implications for our understanding of growth control and antigen processing, and will provide fundamental information regarding the mechanism of receptor trafficking in mammalian cells. ..
- Molecular Analysis of the CCC185 GolginSuzanne Pfeffer; Fiscal Year: 2007..This work has broad implications for our understanding of vesicle docking and fusion events within the secretory and endocytic pathways that are essential for normal human health and disease. ..
- Molecular Analysis of the CCC185 GolginSuzanne Pfeffer; Fiscal Year: 2009..This work has broad implications for our understanding of vesicle docking and fusion events within the secretory and endocytic pathways that are essential for normal human health and disease. ..
- Intracellular Transport: The Mannose Phosphate ReceptorSuzanne Pfeffer; Fiscal Year: 2009..By understanding the molecular events responsible for membrane traffic, we will be better able to intervene in a variety of disease states. ..
- Molecular Analysis of the CCC185 GolginSuzanne R Pfeffer; Fiscal Year: 2010..This work has broad implications for our understanding of vesicle docking and fusion events within the secretory and endocytic pathways that are essential for normal human health and disease. ..
- Intracellular Transport: The Mannose Phosphate ReceptorSuzanne R Pfeffer; Fiscal Year: 2010..By understanding the molecular events responsible for membrane traffic, we will be better able to intervene in a variety of disease states. ..
- LOCALIZATION OF THE GOLGI COMPLEXSuzanne Pfeffer; Fiscal Year: 2001....
- LOCALIZATION OF THE GOLGI COMPLEXSuzanne Pfeffer; Fiscal Year: 1993..This factor has the potential to represent a new class of proteins that can link a molecular motor to a specific membrane-bound organelle...
- Intracellular Transport: The Mannose Phosphate ReceptorSuzanne R Pfeffer; Fiscal Year: 2010..By understanding the molecular events responsible for membrane traffic, we will be better able to intervene in a variety of disease states. ..