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

2010 ◽  
Vol 190 (1) ◽  
pp. 101-114 ◽  
Author(s):  
Poonam R. Molli ◽  
Da-Qiang Li ◽  
Rozita Bagheri-Yarmand ◽  
Suresh B. Pakala ◽  
Hiroshi Katayama ◽  
...  

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.

2003 ◽  
Vol 162 (5) ◽  
pp. 757-764 ◽  
Author(s):  
Yasuhiko Terada ◽  
Yumi Uetake ◽  
Ryoko Kuriyama

A mitosis-specific Aurora-A kinase has been implicated in microtubule organization and spindle assembly in diverse organisms. However, exactly how Aurora-A controls the microtubule nucleation onto centrosomes is unknown. Here, we show that Aurora-A specifically binds to the COOH-terminal domain of a Drosophila centrosomal protein, centrosomin (CNN), which has been shown to be important for assembly of mitotic spindles and spindle poles. Aurora-A and CNN are mutually dependent for localization at spindle poles, which is required for proper targeting of γ-tubulin and other centrosomal components to the centrosome. The NH2-terminal half of CNN interacts with γ-tubulin, and induces cytoplasmic foci that can initiate microtubule nucleation in vivo and in vitro in both Drosophila and mammalian cells. These results suggest that Aurora-A regulates centrosome assembly by controlling the CNN's ability to targeting and/or anchoring γ-tubulin to the centrosome and organizing microtubule-nucleating sites via its interaction with the COOH-terminal sequence of CNN.


2017 ◽  
Vol 56 (38) ◽  
pp. 11409-11414 ◽  
Author(s):  
James A. H. Gilburt ◽  
Hajrah Sarkar ◽  
Peter Sheldrake ◽  
Julian Blagg ◽  
Liming Ying ◽  
...  

2007 ◽  
Vol 13 (14) ◽  
pp. 4098-4104 ◽  
Author(s):  
Charles N. Landen ◽  
Yvonne G. Lin ◽  
Anand Immaneni ◽  
Michael T. Deavers ◽  
William M. Merritt ◽  
...  

2013 ◽  
Vol 8 (10) ◽  
pp. 2184-2191 ◽  
Author(s):  
Fiona C. Rowan ◽  
Meirion Richards ◽  
Rachel A. Bibby ◽  
Andrew Thompson ◽  
Richard Bayliss ◽  
...  

2017 ◽  
Vol 129 (38) ◽  
pp. 11567-11572
Author(s):  
James A. H. Gilburt ◽  
Hajrah Sarkar ◽  
Peter Sheldrake ◽  
Julian Blagg ◽  
Liming Ying ◽  
...  

2021 ◽  
Vol 220 (9) ◽  
Author(s):  
Nicolas Tavernier ◽  
Frank Sicheri ◽  
Lionel Pintard

Aurora A is a serine/threonine kinase essential for mitotic entry and spindle assembly. Recent molecular studies have revealed the existence of multiple, distinct mechanisms of Aurora A activation, each occurring at specific subcellular locations, optimized for cellular context, and primed by signaling events including phosphorylation and oxidation.


2014 ◽  
Author(s):  
Cristina Gutiérrez-Caballero ◽  
Selena G Burgess ◽  
Richard Bayliss ◽  
Stephen J Royle

The interaction between TACC3 (transforming acidic coiled coil protein 3) and the microtubule polymerase ch-TOG (colonic, hepatic tumor overexpressed gene) is evolutionarily conserved. Loading of TACC3–ch-TOG onto mitotic spindle microtubules requires the phosphorylation of TACC3 by Aurora-A kinase and the subsequent interaction of TACC3 with clathrin to form a microtubule-binding surface. Recent work indicates that TACC3 can track the plus-ends of microtubules and modulate microtubule dynamics in non-dividing cells via its interaction with ch-TOG. Whether there is a pool of TACC3–ch-TOG that is independent of clathrin in human cells, and what is the function of this pool, are open questions. Here, we describe the molecular interaction between TACC3 and ch-TOG that permits TACC3 recruitment to the plus-ends of microtubules. This TACC3–ch-TOG pool is independent of EB1, EB3, Aurora-A phosphorylation and binding to clathrin. We also describe the distinct combinatorial subcellular pools of TACC3, ch-TOG and clathrin. TACC3 is often described as a centrosomal protein, but we show that there is no significant population of TACC3 at centrosomes. The delineation of distinct protein pools reveals a simplified view of how these proteins are organized and controlled by post-translational modification.


2002 ◽  
Vol 7 (11) ◽  
pp. 1173-1182 ◽  
Author(s):  
Tomotoshi Marumoto ◽  
Toru Hirota ◽  
Tetsuro Morisaki ◽  
Naoko Kunitoku ◽  
Dongwei Zhang ◽  
...  

2013 ◽  
Vol 289 (1) ◽  
pp. 74-88 ◽  
Author(s):  
Harish C. Thakur ◽  
Madhurendra Singh ◽  
Luitgard Nagel-Steger ◽  
Jana Kremer ◽  
Daniel Prumbaum ◽  
...  

2005 ◽  
Vol 23 (16_suppl) ◽  
pp. 5039-5039 ◽  
Author(s):  
C. N. Landen ◽  
A. Immaneni ◽  
M. T. Deavers ◽  
A. Thornton ◽  
J. Celestino ◽  
...  

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