| First Author | Percival JM | Year | 2004 |
| Journal | Mol Biol Cell | Volume | 15 |
| Issue | 1 | Pages | 268-80 |
| PubMed ID | 14528022 | Mgi Jnum | J:90039 |
| Mgi Id | MGI:3042337 | Doi | 10.1091/mbc.E03-03-0176 |
| Citation | Percival JM, et al. (2004) Targeting of a tropomyosin isoform to short microfilaments associated with the Golgi complex. Mol Biol Cell 15(1):268-80 |
| abstractText | 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. |
