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First published online 15 August 2006
doi: 10.1242/jcs.03147

This Article Figures Only Full Text Full Text (PDF) Supplementary Material All Versions of this Article: jcs.03147v1 119/17/3643    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS 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 Styers, M. L. Articles by Faundez, V. Search for Related Content PubMed PubMed Citation Articles by Styers, M. L. Articles by Faundez, V.

Architecture of the vimentin cytoskeleton is modified by perturbation of the GTPase ARF1

¹ Graduate Program in Biochemistry, Cell, and Developmental Biology, Emory University, Atlanta, GA 30322, USA
² Department of Cell Biology, Emory University, Atlanta, GA 30322, USA
³ Department of Dermatology, Emory University, Atlanta, GA 30322, USA
⁴ Center for Neurodegenerative Diseases, Emory University, Atlanta, GA 30322, USA

^* Author for correspondence (e-mail: faundez{at}cellbio.emory.edu)

Accepted 20 June 2006

Intermediate filaments are required for proper membrane protein trafficking. However, it remains unclear whether perturbations in vesicular membrane transport result in changes in the architecture of the vimentin cytoskeleton. We find that treatment of cells with Brefeldin A, an inhibitor of specific stages of membrane transport, causes changes in the organization of vimentin filaments. These changes arise from movement of pre-existing filaments. Brefeldin A treatment also leads to alterations in the microtubule cytoskeleton. However, this effect is not observed in cells lacking intermediate filaments, indicating that microtubule bundling is downstream of perturbations in the vimentin cytoskeleton. Brefeldin A-induced changes in vimentin architecture are probably mediated through its effects on ADP-ribosylation factor 1 (ARF1). Expression of a dominant-negative mutant of ARF1 induces BFA-like modifications in vimentin morphology. The BFA-dependent changes in vimentin architecture occurred concurrently with the release of the ARF1-regulated adaptor complexes AP-3 and AP-1 from membranes and adaptor redistribution to vimentin networks. These observations indicate that perturbation of the vesicular membrane transport machinery lead to reciprocal changes in the architecture of vimentin networks.

Key words: Vimentin, Intermediate filament, Adaptor, AP-1, AP-3, Brefeldin A, ARF1

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