Abstract
The Cdc42 GTPase binds to numerous effector proteins that control cell polarity, cytoskeletal remodelling and vesicle transport. In many cases the signalling pathways downstream of these effectors are not known. Here we show that the Cdc42 effectors Borg1 to Borg3 bind to septin GTPases. Endogenous septin Cdc10 and Borg3 proteins can be immunoprecipitated together by an anti-Borg3 antibody. The ectopic expression of Borgs disrupts normal septin organization. Cdc42 negatively regulates this effect and inhibits the binding of Borg3 to septins. Borgs are therefore the first known regulators of mammalian septin organization and provide an unexpected link between the septin and Cdc42 GTPases.
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Acknowledgements
We thank P. Silver for the gift of anti-GFP antibody. This work was supported by grants from the National Institutes of Health, DHHS, to I.G.M. and T.J.H.
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This PDF replaces the previous online version published on August 31 2001. Label on Figure 2c has changed from (1-150)GPS-AAA to (1-150)LVL-AAA.
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Joberty, G., Perlungher, R., Sheffield, P. et al. Borg proteins control septin organization and are negatively regulated by Cdc42. Nat Cell Biol 3, 861–866 (2001). https://doi.org/10.1038/ncb1001-861
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DOI: https://doi.org/10.1038/ncb1001-861
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