Phosphorylation of the Par polarity complex protein Par3 at serine 962 is mediated by Aurora A and regulates its function in neuronal polarity

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Abstract

The Aurora kinases are a family of serine/threonine protein kinases that perform important functions during the cell cycle. Recently, it was shown that Drosophila Aurora A also regulates the asymmetric localization of Numb to the basal and the partitioning-defective (Par) complex to the apical cortex of neuroblasts by phosphorylating Par6. Here, we show that Aurora A is required for neuronal polarity. Suppression of Aurora A by RNA interference results in the loss of neuronal polarity. Aurora A interacts directly with the atypical protein kinase C binding domain of Par3 and phosphorylates it at serine 962. The phosphorylation of Par3 at serine 962 contributes to its function in the establishment of neuronal polarity. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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Khazaei, M. R., & Püschel, A. W. (2009). Phosphorylation of the Par polarity complex protein Par3 at serine 962 is mediated by Aurora A and regulates its function in neuronal polarity. Journal of Biological Chemistry, 284(48), 33571–33579. https://doi.org/10.1074/jbc.M109.055897

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