QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

This Article Summary Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fehrenbacher, K. Articles by Pon, L. Search for Related Content PubMed PubMed Citation Articles by Fehrenbacher, K. Articles by Pon, L.

Actin comet tails, endosomes and endosymbionts

Kammy Fehrenbacher^*, Thomas Huckaba^*, Hyeong-Cheol Yang, Istvan Boldogh and Liza Pon

Department of Anatomy and Cell Biology, Columbia University, New York, NY, USA
^* These individuals contributed equally to this manuscript

View larger version (159K): [in a new window]   Fig. 1. Electron microscopy of myosin S1-decorated actin tails of R. conorii (a), L. monocytogenes (b) and S. flexneri (e) in Hep2 cells. The boxes in b and e are shown at higher magnification in (c,d) and (f,g), respectively. Scale bars: 0.2 µm (a,b); 0.4 µm (e); 50 nm (c,d,f,g). Reproduced from Gouin et al. (1999), with permission from Company of Biologists, Ltd.

View larger version (49K): [in a new window]   Fig.·2. PMA (PKC activator phorbol myristate acetate) stimulates the recruitment of N-WASP to vesicles associated with actin comet tails. Cell-free vesicle motility assays containing Xenopus cytosol, membranes and 1 ·µmol·l-1 PMA were fixed in perfusion chambers and immunolabeled with affinity-purified anti-N-WASP antibodies followed by Texas Red-labeled secondary antibodies and FITC–phalloidin. N-WASP and F-actin recruitment occurred in the presence of 75·µmol·l-1 latrunculin A (Lat A), but comet tails were not observed. ToxB treatment prevented both N-WASP and F-actin recruitment, although nonspecific labeling of fixed membranes could be observed with long exposure times. Bar, 5·µm. Reproduced from Taunton et al. (2000), with permission from the Rockefeller University Press.

View larger version (164K): [in a new window]   Fig. 3. Thin-section electron microscopic analysis of vesicles associated with comet tails on endosomes. Cell-free reactions were fixed in perfusion chambers and processed for electron microscopy. A gallery of representative images was assembled to highlight the odd shapes, tubular processes, and multivesicular lumens of vesicles associated with tails. Note the clear circular profiles and mitochondria, none of which are associated with comet tails. Bars, 500 nm. Reproduced from Taunton et al. (2000), with permission from the Rockefeller University Press.

View larger version (33K): [in a new window]   Fig.·4. Colocalization of Arp2p with mitochondria in yeast. Budding yeast cells expressing a fusion protein consisting of the mitochondrial signal sequence of citrate synthase 1 fused to GFP (CS1-GFP) were grown to mid-log phase, fixed with paraformaldehyde and stained for Arp2p using an antibody raised against a conserved peptide sequence found in Arp2p, but not in actin or any other actin-related protein (Moreau et al., 1996). Green, mitochondria visualized using CS1-GFP; red, Arp2p visualized by indirect immunofluorescence. Bar, 1·µm.