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Journal Article

Structural basis for the interaction between the cell polarity proteins Par3 and Par6

MPS-Authors
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Renschler,  FA
Research Group Mechanisms of Ubiquitin-dependent Cell Signaling, Max Planck Institute for Developmental Biology, Max Planck Society;

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Bruekner,  SR
Research Group Mechanisms of Ubiquitin-dependent Cell Signaling, Max Planck Institute for Developmental Biology, Max Planck Society;

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Salomon,  PL
Research Group Mechanisms of Ubiquitin-dependent Cell Signaling, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons273878

Mukherjee,  A
Research Group Mechanisms of Ubiquitin-dependent Cell Signaling, Max Planck Institute for Developmental Biology, Max Planck Society;

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Schütz-Stoffregen,  MC
Research Group Mechanisms of Ubiquitin-dependent Cell Signaling, Max Planck Institute for Developmental Biology, Max Planck Society;

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Henzler,  C
Research Group Mechanisms of Ubiquitin-dependent Cell Signaling, Max Planck Institute for Developmental Biology, Max Planck Society;

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Wiesner,  S
Research Group Mechanisms of Ubiquitin-dependent Cell Signaling, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Renschler, F., Bruekner, S., Salomon, P., Mukherjee, A., Kullmann, L., Schütz-Stoffregen, M., et al. (2018). Structural basis for the interaction between the cell polarity proteins Par3 and Par6. Science Signaling, 11(517): eaam9899. doi:10.1126/scisignal.aam9899.


Cite as: https://hdl.handle.net/21.11116/0000-000A-76AE-E
Abstract
Polarity is a fundamental property of most cell types. The Par protein complex is a major driving force in generating asymmetrically localized protein networks and consists of atypical protein kinase C (aPKC), Par3, and Par6. Dysfunction of this complex causes developmental abnormalities and diseases such as cancer. We identified a PDZ domain-binding motif in Par6 that was essential for its interaction with Par3 in vitro and for Par3-mediated membrane localization of Par6 in cultured cells. In fly embryos, we observed that the PDZ domain-binding motif was functionally redundant with the PDZ domain in targeting Par6 to the cortex of epithelial cells. Our structural analyses by x-ray crystallography and NMR spectroscopy showed that both the PDZ1 and PDZ3 domains but not the PDZ2 domain in Par3 engaged in a canonical interaction with the PDZ domain-binding motif in Par6. Par3 thus has the potential to recruit two Par6 proteins simultaneously, which may facilitate the assembly of polarity protein networks through multivalent PDZ domain interactions.