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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hudson, Andrew M. Cooley, Lynn |
| Description | Author Affiliation: Hudson AM ( Department of Genetics, Yale University School of Medicine, New Haven, CT 06520, USA.) |
| Abstract | The Arp2/3 complex has been shown to dramatically increase the slow spontaneous rate of actin filament nucleation in vitro, and it is known to be important for remodeling the actin cytoskeleton in vivo. We isolated and characterized loss of function mutations in genes encoding two subunits of the Drosophila Arp2/3 complex: Arpc1, which encodes the homologue of the p40 subunit, and Arp3, encoding one of the two actin-related proteins. We used these mutations to study how the Arp2/3 complex contributes to well-characterized actin structures in the ovary and the pupal epithelium. We found that the Arp2/3 complex is required for ring canal expansion during oogenesis but not for the formation of parallel actin bundles in nurse cell cytoplasm and bristle shaft cells. The requirement for Arp2/3 in ring canals indicates that the polymerization of actin filaments at the ring canal plasma membrane is important for driving ring canal growth. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 4 |
| Volume Number | 156 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2002-02-18 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actins Metabolism Cytoskeletal Proteins Insect Proteins Actin-Related Protein 2 Actin-Related Protein 3 Genetics Amino Acid Sequence Animals Biological Transport Cytoplasm Drosophila Genes, Insect Molecular Sequence Data Oogenesis Physiology Ovum Sequence Homology, Amino Acid Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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