I-BAR domains,IRSp53 and filopodium formation |
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| Authors: | Sohail Ahmed Wah Ing Goh Wenyu Bu |
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| Institution: | 1. Institute of Molecular Medicine, National Tsing Hua University, Hsinchu 30013, Taiwan, ROC;2. Department of Medical Science, National Tsing Hua University, Hsinchu 30013, Taiwan, ROC;1. Department of Biophysics, Medical School, University of Pécs, Szigeti str. 12, Pécs H-7624, Hungary;2. Beatson Institute for Cancer Research, Garscube Estate, Switchback Road, Bearsden, Glasgow G61 1BD, UK;3. Szentágothai Research Center, Pécs, Ifjúság str. 34, H-7624, Hungary;4. Hungarian Academy of Sciences, Office for Subsidized Research Units, Budapest, Nádor str. 7, H-1051, Hungary |
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| Abstract: | Filopodia and lamellipodia are dynamic actin-based structures that determine cell shape and migration. Filopodia are thought to sense the environment and direct processes such as axon guidance and neurite outgrowth. Cdc42 is a small GTP-binding protein and member of the RhoGTPase family. Cdc42 and its effector IRSp53 (insulin receptor phosphotyrosine 53 kDa substrate) have been shown to be strong inducers of filopodium formation. IRSp53 consists of an I-BAR (inverse-Bin-Amphiphysin-Rvs) domain, a Cdc42-binding domain and an SH3 domain. The I-BAR domain of IRSp53 induces membrane tubulation of vesicles and dynamic membrane protrusions lacking actin in cells. The IRSp53 SH3 domain interacts with proteins that regulate actin filament formation e.g. Mena, N-WASP, mDia1 and Eps8. In this review we suggest that the mechanism for Cdc42-driven filopodium formation involves coupling I-BAR domain-induced membrane protrusion with SH3 domain-mediated actin dynamics through IRSp53. |
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