© John Wiley & Sons A/S. Published by John Wiley & Sons Ltd
Edited By: Michael S. Marks, Trina A. Schroer, Tom H. Stevens and Sharon A. Tooze
Online ISSN: 1600-0854
Cover Gallery Volume 2
For covers from other volumes, go back to the Cover Gallery index.
Browse the covers of Volume 2 below.
Vol. 2, Iss. 12, Dec 2001
Cover Illustration: Pexophagy in Pichia pastoris. Cells of the methylotrophic yeast P. pastoris were transformed with plasmids encoding the green .uorescent protein fused to SA9/CUT9, and BFP tagged with the peroxisomal targeting signalerine-lysine- leucine (SKL). The cells were grown in methanol to induce peroxisomes that accumulate the BFP-SKLmarker. Subsequently, the cells were shifted to glucose medium ot induce peroxisome degradation. Cells undergoing pexophagy were visualized by .uorescence microscopy after staining the vacuole with the red dye FM4-64.GFP-Gsa9 can be seen to localize to regions of the vacuole in contact with peroxisomes that are in the process of being sequestered during micropexophagy. Stromhaug PE and Klionsky DJ,Traf .c 2001;2:524 - 531.
Vol. 2, Iss. 11, Nov 2001
Cover Illustration: Atomic force microscopy image of a living monolayer of MDCKnCells, viewed in perspective. The artificial color in the image corresponds to sample topography, with the highest point (the nuclei) appearing purple. This image, which was obtained without the use og fixatives or stains, shows several sub-cellular structures, including lamellipodia, intracellular contracts, and nuclei. The image is 145m across in the horizontal dimension (long axis). Image courtesy of Jan Hoh and Cora-ann Schoenberger. Traffic 2 (11): 746.
Vol. 2, Iss. 10, Oct 2001
Cover Illustration: Shiga toxin is accumulated in endosomes of HeLa cells. Cy3-Shiga toxin (red) is retained in early/recycling endosomes after its internalization from the plasma membrane when cells were cooled at 19.5 æ C. The Golgi complex was visualized using antibodies to giantin (green) and the nuclei were labeled with DAPI (blue). (Valderrama et al.Traf .c 2001;2(10):717 –726).
Vol. 2, Iss. 9, Sep 2001
Cover illustration: Proteins such as Ste3p are rapidly degraded after endo-cytosis in the vacuole. Part of the degradation process is the transport of Ste3 into vesicles that bud into the endosomal lumen. These vesicles accumulate in pep4 mutant cells that lack active vacuolar proteases. These vesicles can be visualized by .uorescence using a Ste3-GFP fusion protein (right) or by electron microscopy of isolated vacuoles. (Urbanowski and Piper.Traf .c 2001;29)
Vol. 2, Iss. 8, Aug 2001
Cover illustration: Wild-type yeast (Saccharomyces cerevisiae) haploids at selected stages of cell division. Both the vacuole (red) and mitochondria (green) are transmitted to the bud early in the cell cycle. Transmission of the nucleus is a late event. Vacuole membranes were labeled with FM4–64, mitochondrial membranes were labeled with Mitotracker CMX-ROS, both nuclear and mitochondrial DNA were labeled with DAPI (blue). (Image courtesy of Brian Getting and Lois Weisman, University of Iowa,USA).
Vol. 2, Iss. 7, Jul 2001
Cover illustration: Confocal micrograph of a cultured hippocampal neuron co-stained for the GABAA eceptor in green and GABARAP in ed. GABAA receptors can be seen to form distinct clusters on dendrites that contain only low levels of GABARAP which is localized to internal compartments, some of which co-localize with GABAA receptors intracellular pools. (Image courtesy of Josef Kittler, University College,London).
Vol. 2, Iss. 6, Jun 2001
Cover illustration: Wild-type yeast (Saccharomyces cerevisiae) haploids at selected stages of cell division. Both the vacuole (red) and mitochondria (green) are transmitted to the bud early in the cell cycle. Transmission of the nucleus is a late event. Vacuole membranes were labeled with FM4-64, mitochondrial membranes were labeled with Mitotracker CMX-ROS , both nuclear and mitochondrial DNA were labeled with DAPI (blue). (Image courtesy of Brian Getting and Lois Weisman, University of Iowa, USA).
Vol. 2, Iss. 5, May 2001
Cover illustration: Co-ordination of RhoB¹ endosomes with F-actin. Cells were stained for RhoB (green) and F-actin (red). The RhoB GTPase is localised to the cyto-plasmic face of endocytic vesicles. RhoB stimulates the formation of actin stress fibres and also regulates the intracellular traffic of the EGF receptor. Whilst there is no co-ordination between RhoB+ vesicles and stress fibres, some vesicles are seen to co-localise to patches of polymerised actin. (Image courtesy of Dr. Harry Mellor, University of Bristol, UK).
Vol. 2, Iss. 4, Apr 2001
Cover illustration: Visualization of nucleoid structures within the mitochondrial reticulum in yeast. Yeast cells expressing a GFP-tagged mitochondrial DNA binding protein, Mgm101p (in yellow), were labeled with a mitochondrial-specific vital dye (in red).
Vol. 2, Iss. 3, Mar 2001
Cover illustration: Leishmania promastigote forms expressing GFP-chimeras episomally. Forced overexpression results in the accumulation of excess GFP-chimeras within a unique tubulo-vesicular endosomal compartment (green) in these primitive protozoan parasites. These organisms were treated with a [Red] lipophilic dye (PKH26) to delineate both their cell surface membrane and the membrane lining their flagellar reservoir. The latter is the sole site of both endo-and exocytosis in these highly apically-polarized cells. (see Ghedin et al. Traffic 2001;2(3).)
Vol. 2, Iss. 2, Feb 2001
Cover illustration: Association between mu2 adaptin and the cytoplasmic domain of P-selectin. The signal-binding region of mu2 adaptin was co-crystallized with a peptide corresponding to the COOH-terminal 17 amino acids of human P-selectin, and the structure was determined. The image is a surface representation of mu2 adaptin colored from dark green (high) to gray (low) hydrophobic surface potential with P-selectin peptide bound (shown in purple). The side chains of the tyrosine (Y) and the phenylalanine in the Y+3 position in the peptide bind to the same hydrophobic pockets on the surface of mu2 previously shown to bind other YXX-phi internalization motifs. The leucine in the Y-3 position in the peptide binds to a third hydrophobic pocket not previously recognized as a signal-binding site (see Owen et al., this issue). Submitted by David Owen and Philip R. Evans, MRC Laboratory of Molecular Biology, Cambridge, UK.
Vol. 2, Iss. 1, Jan 2001
Cover illustration: Model depicting putative insulin signalling pathways that regulate GLUT4 trafficking in adipocytes. The background represents a 3T3-L1 adipocyte. Superimposed on this are GLUT4 Storage Vesicles or GSVs the exocytosis of which may be regulated by two separate insulin signalling pathways: one involving IRS-1/PI 3' kinase and Akt, and the other involving a novel adaptor protein CAP that binds to c-Cbl. It is possible that these signalling pathways regulate different steps in GLUT4 exocytosis. Image by J.C. Molero and D.E. James