SPIN90-IRSp53 complex participates in Rac-induced membrane ruffling
| Autor: | Jeonghoon Choi, Yong Seok Kang, Hye Jin Oh, Carmen Teodorof, Woo Keun Song, Jeom Il Bae, Seon-Myung Kim, Jang-Soo Chun |
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| Rok vydání: | 2008 |
| Předmět: |
Membrane ruffling
Genetic Vectors Motility Muscle Proteins RAC1 Nerve Tissue Proteins Biology Transfection SH3 domain Cell Movement Chlorocebus aethiops Animals Humans RNA Small Interfering Cytoskeleton Actin Adaptor Proteins Signal Transducing Platelet-Derived Growth Factor Gene knockdown Cell Membrane Colocalization Cell Biology Cell biology rac GTP-Binding Proteins Gene Knockdown Techniques COS Cells Cell Surface Extensions |
| Zdroj: | Experimental cell research. 315(14) |
| ISSN: | 1090-2422 |
| Popis: | SPIN90 is a key regulator of actin cytoskeletal organization. Using the BioGRID beta database (General Repository for Interaction Datasets), we identified IRSp53 as a binding partner of SPIN90, and confirmed the in vivo formation of a SPIN90–IRSp53 complex mediated through direct association of the proline-rich domain (PRD) of SPIN90 with the SH3 domain of IRSp53. SPIN90 and IRSp53 positively cooperated to mediate Rac activation, and co-expression of SPIN90 and IRSp53 in COS-7 cells led to the complex formation of SPIN90-IRSp53 in the leading edge of cells. PDGF treatment induced strong colocalization of SPIN90 and IRSp53 at membrane protrusions. Within such PDGF-induced protrusions, knockdown of SPIN90 protein using siRNA significantly reduced lamellipodia-like protrusions as well as localization of IRSp53 at those sites. Finally, competitive inhibition of SPIN90-IRSp53 binding by SPIN90 PRD dramatically reduced ruffle formation, further suggesting that SPIN90 plays a key role in the formation of the membrane protrusions associated with cell motility. |
| Databáze: | OpenAIRE |
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