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.
| Original language | English |
|---|---|
| Pages (from-to) | 101-114 |
| Number of pages | 14 |
| Journal | Journal of Cell Biology |
| Volume | 190 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jul 12 2010 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Cell Biology
Cite this
Arpc1b, a centrosomal protein, is both an activator and substrate of Aurora A. / Molli, Poonam R.; Li, Da Qiang; Bagheri-Yarmand, Rozita; Pakala, Suresh B.; Katayama, Hiroshi; Sen, Subrata; Iyer, Jyoti; Chernoff, Jonathan; Tsai, Ming Ying; Nair, Sujit S.; Kumar, Rakesh.
In: Journal of Cell Biology, Vol. 190, No. 1, 12.07.2010, p. 101-114.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Arpc1b, a centrosomal protein, is both an activator and substrate of Aurora A
AU - Molli, Poonam R.
AU - Li, Da Qiang
AU - Bagheri-Yarmand, Rozita
AU - Pakala, Suresh B.
AU - Katayama, Hiroshi
AU - Sen, Subrata
AU - Iyer, Jyoti
AU - Chernoff, Jonathan
AU - Tsai, Ming Ying
AU - Nair, Sujit S.
AU - Kumar, Rakesh
PY - 2010/7/12
Y1 - 2010/7/12
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=77954701718&partnerID=8YFLogxK
U2 - 10.1083/jcb.200908050
DO - 10.1083/jcb.200908050
M3 - Article
VL - 190
SP - 101
EP - 114
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 1
ER -