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Reprogramming Control of an Allosteric Signaling Switch Through Modular Recombination
Abstract
Many eukaryotic signaling proteins are composed of simple modular binding domains, yet they can display sophisticated behaviors such as allosteric gating and multi-input signal integration, properties essential for complex cellular circuits. To understand how such behavior can emerge from combinations of simple domains, we engineered variants of the actin regulatory protein N-WASP (neuronal Wiskott-Aldrich syndrome protein) in which the “output” domain of N-WASP was recombined with heterologous autoinhibitory “input” domains. Synthetic switch proteins were created with diverse gating behaviors in response to nonphysiological inputs. Thus, this type of modular framework can facilitate the evolution or engineering of cellular signaling circuits.
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Cited by
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Tonikian, R., Zhang, Y., Sazinsky, S. L., Currell, B., Yeh, J.-H., Reva, B., Held, H. A., Appleton, B. A., Evangelista, M., Wu, Y., et al. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060239 · Cited by 476
Linear motifs: Evolutionary interaction switches
Neduva, V., & Russell, R. B. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.04.005 · Cited by 352
Xia, Y., DiPrimio, N., Keppel, T. R., Vo, B., Fraser, K., Battaile, K. P., Egan, C., Bystroff, C., Lovell, S., Weis, D. D., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja407644b · Cited by 33
A Designed Zn 2+ Sensor Domain Transmits Binding Information to Transmembrane Histidine Kinases
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Metadata
- Authors
- Dueber, J. E., Yeh, B. J., Chak, K., & Lim, W. A.
- Venue
- Science
- Published
- 2003-09-26
- Volume
- 301
- Issue
- 5641
- Pages
- 1904-1908
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2008472371
- Cited by
- 296
- References
- 0
- FWCI
- 5.15
- Type
- journal article
- Language
- en
- Open access
- closed
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- Dueber, J. E., Yeh, B. J., Chak, K., & Lim, W. A. (2003). Reprogramming Control of an Allosteric Signaling Switch Through Modular Recombination. Science. https://doi.org/10.1126/science.1085945
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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