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Arpc1b, a centrosomal protein, is both an activator and substrate of Aurora A

Poonam R. Molli, Da-Qiang Li, Rozita Bagheri-Yarmand, Suresh B. Pakala, Hiroshi Katayama, Subrata Sen, Jyoti Iyer, Jonathan Chernoff, Ming-Ying Tsai, Sujit S. Nair and Rakesh Kumar
The Journal of Cell Biology
Vol. 190, No. 1 (JULY 12, 2010), pp. 101-114
Stable URL: http://www.jstor.org/stable/27822131
Page Count: 14
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Arpc1b, a centrosomal protein, is both an activator and substrate of Aurora A
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Abstract

Here we provide evidence in support of an inherent role for Arpc1b, a component of the Arp2/3 complex, in regulation of mitosis and demonstrate that its depletion inhibits Aurora A activation at the centrosome and impairs the ability of mammalian cells to enter mitosis. We discovered that Arpc1b colocalizes with γ-tubulin at centrosomes and stimulates Aurora A activity. Aurora A phosphorylates Arpc1b on threonine 21, and expression of Arpc1b but not a nonphosphorylatable Arpc1b mutant in mammalian cells leads to Aurora A kinase activation and abnormal centrosome amplification in a Pak1-independent manner. Together, these findings reveal a new function for Arpc1b in centrosomal homeostasis. Arpc1b is both a physiological activator and substrate of Aurora A kinase and these interactions help to maintain mitotic integrity in mammalian cells.

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