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A more recent version of this article appeared on January 1, 2004
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Submitted on March 26, 2003
Revised on August 8, 2003
Accepted on August 26, 2003
1 Oncology Research Unit, The Children's Hospital at Westmead, Westmead, NSW 2145 Australia; Discipline of Paediatrics and Child Health, University of Sydney, Sydney NSW 4000 Australia; Department of Physiology and Biophysics,
University of Washington, Seattle, 98195-7290, Washington, USA
2 Oncology Research Unit, The Children's Hospital at Westmead, Westmead, NSW 2145 Australia; Discipline of Paediatrics and Child Health, University of Sydney, Sydney NSW 4000 Australia
3 Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072 Australia
4 Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072 Australia; School of Tropical Biology, James Cook University, Townsville, QLD 4811 Australia
5 Oncology Research Unit, The Children's Hospital at Westmead, Westmead, NSW 2145 Australia
6 Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072 Australia; School of Molecular and Microbial Sciences, University of Queensland, Brisbane, QLD 4072 Australia
* Corresponding author. E-mail address: peterg3{at}chw.edu.au.
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
-Tm), but not from either the 
- or 
-Tm genes, are associated
with Golgi-derived vesicles (Heimann et al., 1999). We
now show that Tm5NM-2 is sorted specifically to the Golgi complex while
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.
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