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https://doi.org/10.1371/journal.pone.0012153
Title: | Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: Implications for endocytosis | Authors: | Bu, W. Lim, K.B. Yu, Y.H. Chou, A.M. Sudhaharan, T. Ahmed, S. |
Issue Date: | 2010 | Citation: | Bu, W., Lim, K.B., Yu, Y.H., Chou, A.M., Sudhaharan, T., Ahmed, S. (2010). Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: Implications for endocytosis. PLoS ONE 5 (8) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0012153 | Abstract: | Transducer of Cdc42-dependent actin assembly (Toca-1) consists of an F-BAR domain, a Cdc42 binding site and an SH3 domain. Toca-1 interacts with N-WASP, an activator of actin nucleation that binds Cdc42. Cdc42 may play an important role in regulating Toca-1 and N-WASP functions. We report here that the cellular expression of Toca-1 and N-WASP induces membrane tubulation and the formation of motile vesicles. Marker and uptake analysis suggests that the tubules and vesicles are associated with clathrin-mediated endocytosis. Forster resonance energy transfer (FRET) and Fluorescence Lifetime Imaging Microscopy (FLIM) analysis shows that Cdc42, N-WASP and Toca-1 form a trimer complex on the membrane tubules and vesicles and that Cdc42 interaction with N-WASP is critical for complex formation. Modulation of Cdc42 interaction with Toca-1 and/or N-WASP affects membrane tubulation, vesicle formation and vesicle motility. Thus Cdc42 may influence endocytic membrane trafficking by regulating the formation and activity of the Toca-1/N-WASP complex. © 2010 Bu et al. | Source Title: | PLoS ONE | URI: | http://scholarbank.nus.edu.sg/handle/10635/128863 | ISSN: | 19326203 | DOI: | 10.1371/journal.pone.0012153 |
Appears in Collections: | Staff Publications |
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