Direct interaction between caldesmon and cortactin
| Autor: | Hongqiu Guo, C.-L. Albert Wang, Jolanta Kordowska, Gong-Jie Cao, Renjian Huang |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Binding Sites
biology Biophysics macromolecular substances Plasma protein binding Fibroblasts Biochemistry Calmodulin-binding proteins Article Rats Cell biology Caldesmon Cell cortex biology.protein Animals Calmodulin-Binding Proteins Actin-binding protein Cytoskeleton Cortactin Molecular Biology Cells Cultured Actin Protein Binding |
| Zdroj: | Archives of Biochemistry and Biophysics. 456:175-182 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/j.abb.2006.07.018 |
| Popis: | Actin polymerization and depolymerization plays a central role in controlling a wide spectrum of cellular processes. There are many actin-binding proteins in eukaryotic cells. Their roles in the remodeling of the actin architecture and whether they work cooperatively await further study. Caldesmon (CaD) is an actin-binding protein present in nearly all mammalian cells. Cortactin is another actin-binding protein found mainly in the cell cortex. There have been no reports suggesting that CaD and cortactin interact with each other or work as partners. Here, we present evidence that CaD binds cortactin directly by overlay, pull-down assays, ELISA, and by column chromatography. The interaction involves the N-terminal region of cortactin and the C-terminal region of CaD, and appears to be enhanced by divalent metal ions. Cortactin competes with both full-length CaD and its C-terminal fragment for actin binding. Binding of cortactin partially alleviates the inhibitory effect of CaD on the actomyosin ATPase activity. Not only can binding be demonstrated in vitro, the two proteins also co-localize in activated cells at the cortex. Whether such interactions bear any functional significance awaits further investigation. |
| Databáze: | OpenAIRE |
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