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Published online 5 March 2001. doi:10.1083/jcb.152.5.877
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© The Rockefeller University Press, 0021-9525/2001//877 $5.00
The Journal of Cell Biology, Volume 152, Number 5, , 2001 877-894


Original Article

A Novel Interaction of the Golgi Complex with the Vimentin Intermediate Filament Cytoskeleton



Ya-sheng Gaoa and Elizabeth Sztula

a Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294
Department of Cell Biology, University of Alabama at Birmingham, McCallum Building, Rm. 668, 1530 S. Third Ave., Birmingham, AL 35294-0005.(205) 975-9131(205) 934-1465

esztul{at}uab.edu

The integration of the vimentin intermediate filament (IF) cytoskeleton and cellular organelles in vivo is an incompletely understood process, and the identities of proteins participating in such events are largely unknown. Here, we show that the Golgi complex interacts with the vimentin IF cytoskeleton, and that the Golgi protein formiminotransferase cyclodeaminase (FTCD) participates in this interaction. We show that the peripherally associated Golgi protein FTCD binds directly to vimentin subunits and to polymerized vimentin filaments in vivo and in vitro. Expression of FTCD in cultured cells results in the formation of extensive FTCD-containing fibers originating from the Golgi region, and is paralleled by a dramatic rearrangements of the vimentin IF cytoskeleton in a coordinate process in which vimentin filaments and FTCD integrate into chimeric fibers. Formation of the FTCD fibers is obligatorily coupled to vimentin assembly and does not occur in vim–/– cells. The FTCD-mediated regulation of vimentin IF is not a secondary effect of changes in the microtubule or the actin cytoskeletons, since those cytoskeletal systems appear unaffected by FTCD expression. The assembly of the FTCD/vimentin fibers causes a coordinate change in the structure of the Golgi complex and results in Golgi fragmentation into individual elements that are tethered to the FTCD/vimentin fibers. The observed interaction of Golgi elements with vimentin filaments and the ability of FTCD to specifically interacts with both Golgi membrane and vimentin filaments and promote their association suggest that FTCD might be a candidate protein integrating the Golgi compartment with the IF cytoskeleton.

Key Words: FTCD • vimentin • intermediate filaments • Golgi complex • IFAP



© 2001 The Rockefeller University Press

Abbreviations used in this paper: FTCD, formiminotransferase cyclodeaminase; GFAP, glial fibrillary acid protein; GFP, green fluorescent protein; IF, intermediate filament; IFAP, IF-associated protein; MTOC, microtubule-organizing center; NC, nitrocellulose; NRK, normal rat kidney; SG, stacked Golgi.



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