Kank attenuates actin remodeling by preventing interaction between IRSp53 and Rac1
| Autor: | Ryoiti Kiyama, Badal C. Roy, Naoto Kakinuma |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
rac1 GTP-Binding Protein
Membrane ruffling Nerve Tissue Proteins macromolecular substances Biology Mice Animals Humans Pseudopodia Cytoskeleton Cells Cultured Research Articles Adaptor Proteins Signal Transducing Tumor Suppressor Proteins Actin remodeling Articles Cell Biology Actin cytoskeleton Actins Cell biology Cytoskeletal Proteins Cdc42 GTP-Binding Protein RNA Interference Lamellipodium Carrier Proteins Filopodia HeLa Cells |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.200805147 |
| Popis: | In this study, insulin receptor substrate (IRS) p53 is identified as a binding partner for Kank, a kidney ankyrin repeat–containing protein that functions to suppress cell proliferation and regulate the actin cytoskeleton. Kank specifically inhibits the binding of IRSp53 with active Rac1 (Rac1G12V) but not Cdc42 (cdc42G12V) and thus inhibits the IRSp53-dependent development of lamellipodia without affecting the formation of filopodia. Knockdown (KD) of Kank by RNA interference results in increased lamellipodial development, whereas KD of both Kank and IRSp53 has little effect. Moreover, insulin-induced membrane ruffling is inhibited by overexpression of Kank. Kank also suppresses integrin-dependent cell spreading and IRSp53-induced neurite outgrowth. Our results demonstrate that Kank negatively regulates the formation of lamellipodia by inhibiting the interaction between Rac1 and IRSp53. |
| Databáze: | OpenAIRE |
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