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Cited by 183

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Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck

Open access
Banjade, Sudeep, Wu, Qiong, Mittal, Anuradha, Peeples, William B., Pappu, Rohit V., Rosen, Michael K.·2015·Proceedings of the National Academy of Sciences

Abstract

Significance: Many eukaryotic proteins are composed of tandem arrays of modular domains, which bind peptide ligands that also often appear in tandem arrays. The interdomain linkers in such systems are often considered merely passive elements that flexibly connect the functional domains. Collective interactions among multivalent molecules lead to micron-sized phase-separated states that are thought to be important in cellular organization. Here, we show that in the multivalent signaling adaptor protein Nck, weak interactions involving an interdomain linker play a significant role in self-assembly and phase separation with ligands neuronal Wiskott-Aldrich syndrome protein (N-WASP) and phosphorylated nephrin. Our results suggest that interactions mediated by ordered modular domains may generally act synergistically with weak interactions of disordered interdomain linkers to promote phase separation.

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Metadata

Authors
Banjade, S., Wu, Q., Mittal, A., Peeples, W. B., Pappu, R. V., & Rosen, M. K.
Venue
Proceedings of the National Academy of Sciences
Published
2015-11-09
Volume
112
Issue
47
Pages
E6426-35
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2125272201
Cited by
183
References
3
FWCI
4.63
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck. https://app.cochat.ai/papers/10.1073/pnas.1508778112
The paper
Banjade, S., Wu, Q., Mittal, A., Peeples, W. B., Pappu, R. V., & Rosen, M. K. (2015). Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1508778112

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