Notch receptors are clustered and trans-endocytosed by Delta ligand cells. Confocal micrograph of a Delta expressing cell (left) interacting with a Notch expressing cell (right). Following interaction with Delta (blue), cell surface Notch (yellow) is clustered at cell-cell interfaces. Notch extracellular domain is detected within Delta cells (green) indicative of trans-endocytosis. Endocytosis of ligand while bound to Notch may produce a force sufficient to pull Notch apart and activate signaling.
 
 
 
 
 
 

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Here are the cover illustrations of volume 4 issues. Please click the appropriate link to view the illustrations of previous volumes:

Cover Image
Vol.4 Iss.12, Dec 2003
Cover Illustration: Developmental phenotype of wildtype Dictyostelium cells (left panel) and mutant Dictyostelium cells that lack clathrin light chain (right panel). Dictyostelium cells were inoculated onto an agar plate covered with a lawn of bacteria. After depleting the bacterial lawn, the Dictyostelium cells began their developmental cycle and chemotaxed into mounds of cells. Whereas wildtype cells developed into fruiting bodies formed from a round sorus of spores atop an elongated stalk, cells without clathrin light chain formed elonged spindlystructures. (Wang et al. Traffic 2003; 4(12):891–901).
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Cover Image
Vol.4 Iss.11, Nov 2003
Cover Illustration: The cover shows a confocal immunofluorescence image of the surface of an isolated muscle fibre labeled for the raft proteins caveolin-3 (red) and flotillin-1 (green). The two labels are in completely distinct areas of the sarcolemma. Labeling for caveolin-3 (red) corresponds to areas rich in caveolae, as shown by electron microscopy (insets). For a review of endocytosis by caveolae, 50 years since their discovery, see the article in this issue by Parton and Richards (Traffic 2003;4(11):724–738). Image courtesy of P. Rahkila and R. Parton.
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Cover Image
Vol.4 Iss.10, Oct 2003
Cover Illustration: Image of a CMMT cell that is chronically infected with Mason-Pfizer monkey virus revealing the peri-centriolar assembly site of this prototypic betaretrovirus. Cells were incubated at 20°C for three hours and then fixed and stained for indirect immunofluoresence using antibodies specific for the retroviral Gag protein (red) and λ-tubulin (green). The transport of nascent Gag molecules to the pericentriolar assembly site is described in this issue. An accompanying article describes the surprising role of Env, and its required trafficking through recycling endosomes, in the transport of the assembled capsids away from this assembly site. (See Sfakianos et al. Traffic 4(10):
660–670, and Sfakianos and Hunter. Traffic 4(10):671–680).
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Cover Image
Vol.4 Iss.9, Sept 2003
Cover Illustration: Transmission electron micrograph of a portion of a tobacco BY-2 suspension cell overexpressing a tail-anchored GFP fused to the membrane targeting information of peroxisomal ascorbate peroxidase. Within the cell cytoplasm are homo- and heterotypic aggregates of peroxisomes, plastids, and mitochondria. Lisenbee et al, demonstrate how (mis)sorting and subsequent dimerization of the GFP moieties have confounded the elucidation of an indirect sorting pathway for peroxisomal membrane proteins (Traffic 4(7): 491–501).
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Cover Image
Vol.4 Iss.8, Aug 2003
Cover Illustration: The cover shows a three-dimensional reconstruction of the membranous compartments involved in the formation of peroxisomes in mouse dendritic cells using EM-tomography. ER, dark blue with ribosomes in red, intermediate lamellae, light blue and peroxisomes, green. (See Tabak et al. Traffic 2003;4:512–518).
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Cover Image

Vol.4 Iss.7, July2003
Cover illustration: Transmission electron micrography and electron tomographic images of Chlamydomonas. RIGHT: A transmission electron micrograph of a longitudinal thin section showing a whole Chlamydomonas cell. The basal bodies at the apical region of the cell template the assembly of the two flagella. In wild-type cells, the two flagella are typically 10-12 microns in length. Only the basal portions of two flagella are shown in this thin section. LEFT: Electron tomography was used to extract structural detail of organelles in the cell at 5-10 nm resolution in 3-D. Shown on the left are selected tomographic slices through cross-sections of the basal body and transition zone.
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Cover Image
Vol.4 n.6, June 2003
Cover illustration: Transmission electron micrograph of an Adenovirus type 2 particle docked to cytoplasmic filaments of a nuclear pore complex in a human epithelial cell 60 min post infection. The image is 750 nm across the horizontal axis. Photograph by Karin Boucke & Urs Greber, University of Zürich. (Traffic 2003 4(6): 390–402). See also Nature Cell Biology 2001;3:1092–1100.
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Cover Image
Vol.4 Iss.5, May 2003
Cover illustration: Assessing the polarity of the Golgi apparatus. A preparation of isolated rat Golgi was fixed and processed for cryoultramicrotomy. Frozen sections were double-labeled with an antibody against the matrix protein GM130 (5 nm gold) and the lectin Ricinus communis agglutinin I (10 nm gold) that binds specifically to galactose residues. Note that the GM130 labeling decorates nearly exclusively one side of the stack, the cis-Golgi, whereas the lectin labeling starts appearing only in the medial Golgi and is most concentrated on the trans cisterna and the trans-Golgi network. For more information on these experiments, see article by Taguchi, Pypaert and Warren, in this issue. (Photograph courtesy of Marc Pypaert).
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Cover Image
Vol.4 Iss.4, April 2003
Cover illustration: An SKBR-3 breast cancer cell is shown, with a green-fluorescent protein (GFP) fusion of the Grp1 pleckstrin homology (PH) domain bound to phosphatidylinositol-3,4,5 trisphosphate (PtdIns(3,4,5)P3) at its plasma membrane. Superimposed in the foreground is a surface representation of the Grp1 PH domain crystal structure bound to a single PtdIns(3,4,5)P3 molecule (with headgroup in red and yellow). Details of Grp1 PH domain binding to the membrane are discussed in the review by Lemmon (Traffic 2003; 4:201–203). Image courtesy of Mitchell Berger, Kathryn Ferguson, and Mark Lemmon, University of Pennsylvania.
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Cover Image
Vol.4 Iss.3, March 2003
Cover Illustration: Expression of an N-terminal truncation mutant (NT-GAIP-GFP) of the RGS protein, GAIP in HeLa cells. NT-GAIP induces tubulation of trans-Golgi Network derived membranes which represent a transport intermediate of the post-Golgi exocytic transport pathway (Wylie et al. Traffic 2003; 4:175–189). The tubules are clearly visible extending long distances in these fluorescent and embossed images of transfected HeLa cells.
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