Traffic

Cover image for Vol. 19 Issue 1

Edited By: Michael S. Marks, Trina A. Schroer, Robert G. Parton and Sharon A. Tooze

Online ISSN: 1600-0854

Cover Gallery Volume 5


Volume 5

For covers from other volumes, go back to the Cover Gallery index.

Browse the covers of Volume 5 below.

Cover Image

Vol. 5, Iss. 12, Dec 2004

Cover Illustration: 3-D reconstructions of multilaminar lysosomes reveal the organization of their internal membranes. Top three images: the left image shows a slice through the electron tomographic reconstruction of a multilaminar lysosome in a human dendritic cell. The middle image shows how the membranes in the tomographic slices were traced to create a 3-D model. The right image shows a 3-D model of the multilaminar lysosome that is projected on top of a tomographic slice. Lower image: 3-D model of half of the multilaminar lysosome, showing the onion-like organization of the internal membranes. The cell was preserved by high-pressure freezing, freeze substitution and embedding in epon (see Murk et al. 2004; 5(12):936-945).
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Cover Image

Vol. 5, Iss. 11, Nov 2004

Cover Illustration: Cover Legend: Recent evidence indicates that mutants of the gonadotropin releasing hormone (GnRH) receptor associated with disease are mis-folded and become misrouted proteins; these can be correctly routed and restored to function by pharmacological chaperones which correct the folding error and allow mutant proteins to escape the cell's quality control apparatus. Because this is found to be the case for other proteins as well, these results challenge the conventional view that all mutants are defective in function and suggest that many are simply misrouted. Accordingly, new therapeutic approaches are suggested requiring an understanding of cellular trafficking. (See Ulloa-Aguirre et al. Traffic 2004;5(11):821–837.)
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Cover Image

Vol. 5, Iss. 10, Oct 2004

Cover Illustration: Myosin-VI localization is regulated by its adaptor proteins. Upper left: In the epithelial cell line ARPE-19, clathrin-coated endocytic vesicles are labeled with AP-2 (red). Myosin-VI (green) localizes to a separate population of uncoated endocytic vesicles in the cell peripheries. Lower left: Dab2 is an adaptor protein that binds to clathrin as well as myosin-VI. When Dab2 (red) is overexpressed in ARPE-19 cells, the tail of myosin-VI (green) is rerouted to clathrin-coated structures. Right: GIPC is a myosin-VI-binding adaptor protein that normally tethers myosin-VI to uncoated vesicles. When Dab2 (red), GIPC (green), and the tail of myosin-VI (blue) are all overexpressed in ARPE-19 cells, the myosin-VI tail bridges Dab2 and GIPC, leading to formation of a ternary complex that localizes to clathrin-coated vesicles. This complex may form transiently as endocytic vesicles uncoat, allowing efficient recruitment of myosin-VI and GIPC to the surface of the newly uncoated vesicle (see Dance et al., Traffic 2004; 5(10):798-813).
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Cover Image

Vol. 5, Iss. 9, Sep 2004

Cover Illustration: Low power Nomarski image showing a virological synapse between two CD4 target T-cells (red) and an HIV JurkatLAI effector T-cell (unstained or green). CD4 is red, HIV Env is green and regions of colocalisation of receptors appear yellow. (See Jolly and Sattentau, Traffic 2004; 5(9):643–650 )
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Cover Image

Vol. 5, Iss. 8, Aug 2004

Cover Illustration: Cells expressing a single open reading frame encoding a self-processing polyprotein. Proteins were concatenated via a short (24aa) auto-’cleaving’ peptide. By the inclusion of targeting signals at multiple sites within the polyprotein, individual processing products were targeted to different sites. Here, YFP is localised in the Golgi apparatus, whilst heamaggutinin-neuraminidase (red) is independently targeted to the surface of the cell. (DeFiore and Ryan. Traffic 2004; 5(8): 616–626).
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Cover Image

Vol. 5, Iss. 7, Jul 2004

Cover Illustration: Caenorhabditis elegans male copulatory apparatus (ventral view) showing the cuticular fan, the supporting rays and two central spicules. Transgenic worms carrying a GFP fusion with the neuroendocrine dense core vesicle protein IDA-1 show abundant expression in the three neuronal cell bodies innervating the structure bright punctae in neuronal processes emanating from the organ. The punctae appear to correspond to dense core vesicle (DCV) of peptidergic neurons and endocrine cells and are move at velocities up to 4 µ/s in a kinesin-dependent manner (Zahn et al, Traffic 2004; 5(7):544–559).
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Cover Image

Vol. 5, Iss. 6, Jun 2004

Cover Illustration: Chlamydia trachomatiselementary body (green) at the apex of an actin-rich pedestral prior to internalization. Chlamydiae are bacterial obligate intracellular pathogens that efficiently trigger endocytosis through a process that involves localized recruitment of actin and the formation of a pedestal-like structure at the immediate site of attachment and entry. Once internalized, chlamydiae remain within a membrane bound vesicle for the duration of their intracellular developmental cycle. (Image courtesy of Elizabeth R. Fischer, Rocky Mountain Laboratories, Hamilton, see Carabeo et al. Traffic 2004; 5(6): 418–425).
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Cover Image

Vol. 5, Iss. 5, May 2004

Cover Illustration: Structurally re-defining the trans-Golgi network by EM tomography. At the trans-face of the mammalian Golgi complex, multiple cisternae - frequently referred to as the trans- Golgi network (TGN) - detach and fragment as membrane is consumed in the process of packaging cargo for exit. In mammalian cells that make and secrete insulin (left and middle, HIT-T15 cells; right, beta cell in situ in an islet of Langerhans isolated from mouse pancreas), the two trans-most cisternae are structurally as well as functionally distinct. The penultimate trans-most cisterna (gold) is frequently the most structurally variegated cisterna and has a tubular, network-like appearance. The trans-most cisterna (bright red) exhibits only clathrin-coated profiles and is the only cisterna with clathrin-coated buds (Image courtesy of Dr. Brad Marsh, Institute for Molecular Bioscience, Brisbane, Australia, see Mogelsvang et al.Traffic 5(5):337-344.).
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Cover Image

Vol. 5, Iss. 4, Apr 2004

Cover Illustration: Lck, a raft-philic Src-family kinase, enters and exits the region of the T-cell receptor (TCR) cluster induced by aggregated antibodies (the region surrounded by the red contour). Lck conjugated with GFP was expressed in a Jurkat cell and its distribution 5 min after local TCR stimulation was observed (upper left). The overall distribution indicates concentration of Lck-GFP on and around the TCR cluster, but single fluorescent molecule video imaging data on the right clearly indicates that Lck-GFP molecules frequently enter and exit the TCR cluster region (single Lck-GFP molecule trajectories for 0.66 s are superimposed on the image). Lck movement is regulated by the presence of the actin-based membrane-skeleton "fence" and anchored-protein "pickets", and the diffusion rate of Lck-GFP is decreased toward the TCR cluster site (A TCR cluster shown in the right bottom corner of the cartoon) due to the denser meshwork of the actin filaments (the membrane skeleton meshwork, the cartoon on the lower left). For more details, see Kusumi et al. (Traffic 2004; 5(4): 213–230) and Ike et al. (Chemphyschem 2003; 4:620–626). Image courtesy of Hiroshi Ike, Junko Kondo, and Akihiro Kusumi.
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Cover Image

Vol. 5, Iss. 3, Mar 2004

Cover Illustration: Clathrin Heavy Chains in Human Skeletal Muscle.
Human skeletal muscle was prepared for immunofluorescence analysis using antibodies specific for conventional clathrin heavy chain, CHC17 (green) and the isoform of clathrin heavy chain, that is highly expressed in skeletal muscle, CHC22 (red). It can be seen that the two staining patterns do not overlap suggesting unique functions of the two proteins (Towler et al., Traffic 2004; 5(3): 129–139).
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Cover Image

Vol. 5, Iss. 2, Feb 2004

Cover Illustration: Structure of the Cover Image-COP appendage domain with the residues of the putative ARFGAP2 binding pocket highlighted (V772, Q784,W776, F829, R843, R859).
The structure is superimposed on a Vero cell labelled for COPI by immunofluorescence, to show the localization of native COPI. An affinity-purified anti-Cover Image-COP peptide antibody raised in rabbits (anti-”EAGE”; see Duden et al., 1991; Cell 64, 649-665) was used to visualize COPI-decorated Golgi complex and intermediate compartment membranes in methanol/acetone-fixed Vero cells (Image courtesy of Dr. Irina Majoul, CIMR Cambridge, see Watson et al. Traffic 2004; 5(2): 79-88.).
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