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Genomes and Genes | S R PfefferSummaryAffiliation: Stanford University Country: USA Publications
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Publications
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...- Membrane transport: retromer to the rescueS R Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
Curr Biol 11:R109-11. 2001..Orthologs of these proteins in mammalian cells are likely to play a similar role but their cargoes are yet to be identified... 
Constructing a Golgi complexS R Pfeffer
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA
J Cell Biol 155:873-5. 2001..These findings suggest that Golgin-45 serves as a linchpin for the maintenance of Golgi complex structure, and offer hints as to the mechanisms by which the polarized Golgi complex is constructed...- Rab GTPases: specifying and deciphering organelle identity and functionS R Pfeffer
Dept of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Trends Cell Biol 11:487-91. 2001..Rabs organize distinct protein scaffolds within a single organelle and act in a combinatorial manner with their effectors to regulate all stages of membrane traffic... - Biochemical characterization of mapmodulin, a protein that binds microtubule-associated proteinsN Ulitzur
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
J Biol Chem 272:30577-82. 1997..Finally, despite identity in polypeptide sequence with a protein reported to act as an inhibitor of protein phosphatase 2A, native mapmodulin was not able to inhibit protein phosphatase 2A in Chinese hamster ovary cell cytosol... - Role of Rab9 GTPase in facilitating receptor recruitment by TIP47K S Carroll
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Science 292:1373-6. 2001..Thus, a cytosolic cargo selection device may be selectively recruited onto a specific organelle, and vesicle budding might be coupled to the presence of an active Rab GTPase... - Quantitative analysis of TIP47-receptor cytoplasmic domain interactions: implications for endosome-to-trans Golgi network traffickingJ P Krise
Department of Biochemistry, Stanford University School of Medicine, CA 94305 5307, USA
J Biol Chem 275:25188-93. 2000..Moreover, our data suggest unexpectedly that furin, TGN38, and carboxypeptidase D may use a distinct vesicular carrier and perhaps a distinct route for transport between endosomes and the trans Golgi network... - Recognition of the 300-kDa mannose 6-phosphate receptor cytoplasmic domain by 47-kDa tail-interacting proteinJ G Orsel
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Proc Natl Acad Sci U S A 97:9047-51. 2000..Although crystallography will be needed to define the precise interaction interface, these data provide an initial structural basis for TIP47-CI-MPR association... - A novel assay reveals a role for soluble N-ethylmaleimide-sensitive fusion attachment protein in mannose 6-phosphate receptor transport from endosomes to the trans Golgi networkC Itin
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
J Biol Chem 272:27737-44. 1997..Together with alpha-SNAP, NSF can increase the extent of transport. These data show that alpha-SNAP, a soluble component of the SNAP receptor machinery, facilitates transport from endosomes to the trans Golgi network... - A novel Rab9 effector required for endosome-to-TGN transportE Diaz
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
J Cell Biol 138:283-90. 1997..These data are consistent with a model in which p40 and Rab9 act together to drive the process of transport vesicle docking... - TIP47: a cargo selection device for mannose 6-phosphate receptor traffickingE Diaz
Department of Biochemistry, Stanford University School of Medicine, California 94305 5307, USA
Cell 93:433-43. 1998..These data suggest that TIP47 binds MPR cytoplasmic domains and facilitates their collection into transport vesicles destined for the Golgi... - Mapmodulin: a possible modulator of the interaction of microtubule-associated proteins with microtubulesN Ulitzur
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Proc Natl Acad Sci U S A 94:5084-9. 1997..To our knowledge, mapmodulin represents the first example of a protein that can bind and potentially regulate multiple MAP proteins... - Characterization of a 76 kDa endosomal, multispanning membrane protein that is highly conserved throughout evolutionF Schimmöller
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 5307, USA
Gene 216:311-8. 1998..The structural features of p76 suggest that it may function as a channel or small molecule transporter in intracellular compartments throughout phylogeny. 1998 Elsevier Science B.V... - 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... - TIP47 is not a component of lipid dropletsP Barbero
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 95307, USA
J Biol Chem 276:24348-51. 2001..Using antibodies specific for residues 152-434 of TIP47, we show that TIP47 is not a constituent of lipid droplets... - Receptor extracellular domains may contain trafficking information. Studies of the 300-kDa mannose 6-phosphate receptorS M Dintzis
Department of Biochemistry, Stanford University School of Medicine, California 94305 5307
J Biol Chem 269:12159-66. 1994..These experiments suggest that the presence of the mannose 6-phosphate receptor extracellular domain may interfere with the rapid recycling of receptors from early endosomes to the cell surface and detain receptors within endosomes... - Rab GDI: a solubilizing and recycling factor for rab9 proteinT Soldati
Department of Biochemistry, Stanford University School of Medicine, California 94028
Mol Biol Cell 4:425-34. 1993..Thus GDI proteins have the potential to regulate the availability of specific intracellular transport factors... - Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-alpha, and guanine nucleotidesA D Shapiro
Department of Biochemistry, Stanford University School of Medicine, California 94305 5307, USA
J Biol Chem 270:11085-90. 1995..Finally, a previously uncharacterized minor form of GDI-alpha inhibited GDP dissociation from prenyl Rab9 by 1.9-fold and bound prenyl Rab9 with a KD of 67 nM in 0.1% Lubrol... - 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... - 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... - Rab GTPases, directors of vesicle dockingF Schimmöller
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305 5307, USA
J Biol Chem 273:22161-4. 1998 - 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... - Rab7 and Rab9 are recruited onto late endosomes by biochemically distinguishable processesT Soldati
Department of Biochemistry, Stanford University School of Medicine, California 94305 5307, USA
J Biol Chem 270:25541-8. 1995..Since Rab7 and Rab9 are both localized at least in large part, to late endosomes, this suggests that a single organelle may bear multiple Rab recruitment machines... - 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... - 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... - 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... - 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... - 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... - 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... - 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... - 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.... - 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... - 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... 
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... - 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... - 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...