Abstract
Background: Tropomodulin is a tropomyosin-dependent actin-capping protein. Results: Mutations intropomodulin-1 that reduce its affinity for tropomyosin (R11K, D12N, Q144K) reduced inhibition of actin pointed-end polymerization in vitro and decreased assembly of tropomodulin-1 in skeletal myocytes. Conclusion: The tropomyosin-binding ability of tropomodulin-1 directly influences its actin filament regulatory activity. Significance: Creating a tool for studying the roles of different tropomodulin isoforms in living cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4899-4907 |
| Number of pages | 9 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 7 |
| DOIs | |
| State | Published - Feb 15 2013 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology