In addition to its function as an Arp2/3 complex subunit, Arp1cb interacts with and stimulates Aurora A at centrosomes, functioning in cell cycle progression

Ando

Barros

Bayliss

Crosio

Da-Qiang Li

Fielding

Gachet

Gerisch

Goley

Hiroshi Katayama

Hirota

Humphries

Hurst

Hutterer

Igarashi

Jonathan Chernoff

Jyoti Iyer

Katayama

Kumar

Littlepage

Machesky

Macůrek

Mahlamäki

Marumoto

Mazumdar

Meijerman

Menard

Ming-Ying Tsai

Mori

Ouchi

Poonam R. Molli

Pugacheva

Rakesh Kumar

Rozita Bagheri-Yarmand

Sankaran

Sasai

Scrittori

Stenoien

Subrata Sen

Sujit S. Nair

Suresh B. Pakala

Tsai

Vadlamudi

Walter

Yang

Zhao

Zhou

Zigmond

English

PubMed

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.</jats:p

Crossref

The Journal of Cell Biology

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

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http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2911675

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

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