Abstract
Dynactin is a large multiprotein complex that contains at least nine different polypeptide subunits. Ultrastructural analysis reveals two domains, a short filament of the actin-related protein Arpl (aka centractin) and a projecting sidearm thought to participate in dynein binding Previous work (Echeverri et al, J Cell Biol, 1996) indicates that overexpression of the 50kD dynactin subunit (dynamitin) causes the sidearm to dissociate from the Arp 1 filament which leads to disruptions in mitosis and membranous organelle localization, specifically Golgi and endosomes. We have found that, although the overall organization of the microtubule network in interphase cells is maintained, the structure and function of centrosomes are also disrupted by dynamitin overexpression. Real time observation of the dynamics of early and late endosomal markers reveal defects in endosomal motility while virus infection studies indicate that endocytic trafficking is perturbed. We have also analyzed the effects of overexpressing other dynactin subunits (p24, p62, p!50Glued or its subdomains) on mitotic progression, centrosome function and membranous organelle localization. These results suggest a novel model of the dynactin-cargo interaction.
| Original language | English (US) |
|---|---|
| Journal | FASEB Journal |
| Volume | 11 |
| Issue number | 9 |
| State | Published - 1997 |
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ASJC Scopus subject areas
- Agricultural and Biological Sciences (miscellaneous)
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Cell Biology
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Dynactin and cytoplasmic dynein-based motility. / Bineham, J. B.; Duiardin, A. D.; Gill, S. R.; Ouintvne, N.; Valelti, C.; Wetzel, D.; Demey, A. J.; Kreis, T.; Schroer, T. A.
In: FASEB Journal, Vol. 11, No. 9, 1997.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dynactin and cytoplasmic dynein-based motility
AU - Bineham, J. B.
AU - Duiardin, A. D.
AU - Gill, S. R.
AU - Ouintvne, N.
AU - Valelti, C.
AU - Wetzel, D.
AU - Demey, A. J.
AU - Kreis, T.
AU - Schroer, T. A.
PY - 1997
Y1 - 1997
N2 - Dynactin is a large multiprotein complex that contains at least nine different polypeptide subunits. Ultrastructural analysis reveals two domains, a short filament of the actin-related protein Arpl (aka centractin) and a projecting sidearm thought to participate in dynein binding Previous work (Echeverri et al, J Cell Biol, 1996) indicates that overexpression of the 50kD dynactin subunit (dynamitin) causes the sidearm to dissociate from the Arp 1 filament which leads to disruptions in mitosis and membranous organelle localization, specifically Golgi and endosomes. We have found that, although the overall organization of the microtubule network in interphase cells is maintained, the structure and function of centrosomes are also disrupted by dynamitin overexpression. Real time observation of the dynamics of early and late endosomal markers reveal defects in endosomal motility while virus infection studies indicate that endocytic trafficking is perturbed. We have also analyzed the effects of overexpressing other dynactin subunits (p24, p62, p!50Glued or its subdomains) on mitotic progression, centrosome function and membranous organelle localization. These results suggest a novel model of the dynactin-cargo interaction.
AB - Dynactin is a large multiprotein complex that contains at least nine different polypeptide subunits. Ultrastructural analysis reveals two domains, a short filament of the actin-related protein Arpl (aka centractin) and a projecting sidearm thought to participate in dynein binding Previous work (Echeverri et al, J Cell Biol, 1996) indicates that overexpression of the 50kD dynactin subunit (dynamitin) causes the sidearm to dissociate from the Arp 1 filament which leads to disruptions in mitosis and membranous organelle localization, specifically Golgi and endosomes. We have found that, although the overall organization of the microtubule network in interphase cells is maintained, the structure and function of centrosomes are also disrupted by dynamitin overexpression. Real time observation of the dynamics of early and late endosomal markers reveal defects in endosomal motility while virus infection studies indicate that endocytic trafficking is perturbed. We have also analyzed the effects of overexpressing other dynactin subunits (p24, p62, p!50Glued or its subdomains) on mitotic progression, centrosome function and membranous organelle localization. These results suggest a novel model of the dynactin-cargo interaction.
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M3 - Article
AN - SCOPUS:33750275600
VL - 11
JO - FASEB Journal
JF - FASEB Journal
SN - 0892-6638
IS - 9
ER -