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Originally published as MBC in Press, 10.1091/mbc.E03-03-0176 on October 3, 2003

Vol. 15, Issue 1, 268-280, January 2004

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Targeting of a Tropomyosin Isoform to Short Microfilaments Associated with the Golgi Complex

Justin M. Percival * {dagger} {ddagger}, Julie A. I. Hughes * {dagger}, Darren L. Brown §, Galina Schevzov * {dagger}, Kirsten Heimann § ¶, Bernadette Vrhovski *, Nicole Bryce * {dagger}, Jennifer L. Stow § ||, and Peter W. Gunning * {dagger} #

* Oncology Research Unit, The Children's Hospital at Westmead, Westmead, NSW 2145, Australia; {dagger} Discipline of Paediatrics and Child Health, University of Sydney, Sydney, NSW 2006, Australia; § Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia; and || School of Molecular and Microbial Sciences, University of Queensland, Brisbane, QLD 4072, Australia

Submitted March 26, 2003; Revised August 8, 2003; Accepted August 26, 2003
Monitoring Editor: David Drubin

A growing body of evidence suggests that the Golgi complex contains an actin-based filament system. We have previously reported that one or more isoforms from the tropomyosin gene Tm5NM (also known as {gamma}-Tm), but not from either the {alpha}- or {beta}-Tm genes, are associated with Golgi-derived vesicles (Heimann et al., (1999). J. Biol. Chem. 274, 10743-10750). We now show that Tm5NM-2 is sorted specifically to the Golgi complex, whereas Tm5NM-1, which differs by a single alternatively spliced internal exon, is incorporated into stress fibers. Tm5NM-2 is localized to the Golgi complex consistently throughout the G1 phase of the cell cycle and it associates with Golgi membranes in a brefeldin A-sensitive and cytochalasin D-resistant manner. An actin antibody, which preferentially reacts with the ends of microfilaments, newly reveals a population of short actin filaments associated with the Golgi complex and particularly with Golgi-derived vesicles. Tm5NM-2 is also found on these short microfilaments. We conclude that an alternative splice choice can restrict the sorting of a tropomyosin isoform to short actin filaments associated with Golgi-derived vesicles. Our evidence points to a role for these Golgi-associated microfilaments in vesicle budding at the level of the Golgi complex.

Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03-03-0176. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03-03-0176.

Abbreviations used: BFA, brefeldin A; Tm, tropomyosin; ARF, ADP-ribosylation factor.

{ddagger} Present address: Department of Physiology and Biophysics, University of Washington, Seattle, WA 98195-7290

Present address: School of Tropical Biology, James Cook University, Townsville, QLD 4811, Australia.

# Corresponding author. E-mail address: peterg3{at}chw.edu.au.




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