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First published online August 24, 2006

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Vimentin caught in membrane traffic jam

The cytoskeleton has important roles in membrane trafficking, providing tracks for vesicle transport and helping to maintain the integrity of various organelles. Intermediate filaments such as vimentin play their part and are required for vesicle transport and positioning of endosomes and lysosomes. On p. 3643, Victor Faundez and co-workers show that the reverse is also true: intermediate filament architecture depends on vesicle transport. They find that treatment of cells with brefeldin A (BFA), which blocks various steps in membrane trafficking, also disrupts the vimentin network. The authors demonstrate that the effect is not due to global changes in morphology or Golgi fragmentation induced by BFA. Moreover, they can mimic it by treating cells with mutant forms of ARF1, a small GTPase that regulates vesicle budding. Interestingly, the changes in vimentin architecture involve the reorganization of pre-existing filaments into bundles and are accompanied by relocation of ARF-1-regulated membrane adaptor complexes (AP1 and AP3) to the vimentin network. These findings thus reveal a reciprocal relationship between filament architecture and membrane trafficking and raise the possibility that adaptor proteins recruit factors that bundle intermediate filaments.

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Related articles in JCS:

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

Melanie L. Styers, Andrew P. Kowalczyk, and Victor Faundez
JCS 2006 119: 3643-3654. [Abstract] [Full Text]  

This Article Full Text (PDF) 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 Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?