Targeting of a tropomyosin isoform to short microfilaments associated with the Golgi complex

Percival, J. M., Hughes, J. A. I., Brown, D. L., Schevzov, G., Heimann, K., Vrhovski, B., Bryce, N., Stow, J. L. and Gunning, P. W. (2004) Targeting of a tropomyosin isoform to short microfilaments associated with the Golgi complex. Molecular Biology of The Cell, 15 1: 268-280. doi:10.1091/mbc.E03-03-0176

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Author Percival, J. M.
Hughes, J. A. I.
Brown, D. L.
Schevzov, G.
Heimann, K.
Vrhovski, B.
Bryce, N.
Stow, J. L.
Gunning, P. W.
Title Targeting of a tropomyosin isoform to short microfilaments associated with the Golgi complex
Journal name Molecular Biology of The Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2004
Sub-type Article (original research)
DOI 10.1091/mbc.E03-03-0176
Open Access Status File (Publisher version)
Volume 15
Issue 1
Start page 268
End page 280
Total pages 13
Place of publication Bethesda
Publisher American Society for Cell Biology
Collection year 2004
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
780106 Political science and public policy
Abstract 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.
Keyword Cell Biology
Constitutive Transport Vesicles
Messenger-rna
Myosin-ii
Endoplasmic-reticulum
Molecular Composition
Actin Microfilaments
Proteins
Identification
Localization
Muscle
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 04:39:32 EST