scholarly journals Phosphorylation of the Carboxyl Terminus of Inner Centromere Protein (INCENP) by the Aurora B Kinase Stimulates Aurora B Kinase Activity

2002 ◽  
Vol 277 (31) ◽  
pp. 27577-27580 ◽  
Author(s):  
John D. Bishop ◽  
Jill M. Schumacher
Keyword(s):  
Kinase Activity ◽  
Carboxyl Terminus ◽  
Aurora B ◽  
Aurora B Kinase ◽  
Centromere Protein

scholarly journals CENP-I and Aurora B act as a molecular switch that ties RZZ/Mad1 recruitment to kinetochore attachment status

2014 ◽  
Vol 205 (4) ◽  
pp. 541-554 ◽  
Author(s):  
Daniel R. Matson ◽  
P. Todd Stukenberg
Keyword(s):  
Kinase Activity ◽  
Spindle Checkpoint ◽  
Molecular Switch ◽  
Aurora B ◽  
Aurora B Kinase ◽  
Dynamic Regulation ◽  
Checkpoint Proteins ◽  
Centromere Protein ◽  
Stable Association ◽  
Checkpoint Signal

The RZZ (Rod, ZW10, and Zwilch) complex and Mad1 proteins tightly associate with kinetochores to generate the spindle checkpoint signal, but they are released when a kinetochore forms mature microtubule attachments. Here we demonstrate that the centromere protein CENP-I is required to generate a stable association of RZZ and Mad1 with kinetochores. CENP-I also inhibits their removal by dynein stripping. This regulation of Mad1 and RZZ dissociation functions independently of Aurora B, which regulates their association. We show that the microtubule status of each kinetochore independently dictates the recruitment of Aurora B kinase, kinase activity on a kinetochore substrate, and loading of spindle checkpoint proteins. This dynamic regulation of Mad1 association by Aurora B is only uncovered when CENP-I is depleted, consistent with our finding that CENP-I inhibits the dissociation of Mad1. We conclude that the dual activities of Aurora B and CENP-I generate a molecular switch that maintains a robust spindle checkpoint signal at prometaphase kinetochores until they attain mature attachments to microtubules.

scholarly journals Aurora B kinase activity is regulated by SET/TAF1 on Sgo2 at the inner centromere

2019 ◽  
Vol 218 (10) ◽  
pp. 3223-3236 ◽  
Author(s):  
Yuichiro Asai ◽  
Koh Fukuchi ◽  
Yuji Tanno ◽  
Saki Koitabashi-Kiyozuka ◽  
Tatsuyuki Kiyozuka ◽  
...  
Keyword(s):  
Chromosome Segregation ◽  
Chromosomal Instability ◽  
Kinase Activity ◽  
Fine Tuning ◽  
Aurora B ◽  
The Novel ◽  
Aurora B Kinase ◽  
Microtubule Attachment ◽  
Molecular Events

The accurate regulation of phosphorylation at the kinetochore is essential for establishing chromosome bi-orientation. Phosphorylation of kinetochore proteins by the Aurora B kinase destabilizes improper kinetochore–microtubule attachments, whereas the phosphatase PP2A has a counteracting role. Imbalanced phosphoregulation leads to error-prone chromosome segregation and aneuploidy, a hallmark of cancer cells. However, little is known about the molecular events that control the balance of phosphorylation at the kinetochore. Here, we show that localization of SET/TAF1, an oncogene product, to centromeres maintains Aurora B kinase activity by inhibiting PP2A, thereby correcting erroneous kinetochore–microtubule attachment. SET localizes at the inner centromere by interacting directly with shugoshin 2, with SET levels declining at increased distances between kinetochore pairs, leading to establishment of chromosome bi-orientation. Moreover, SET overexpression induces chromosomal instability by disrupting kinetochore–microtubule attachment. Thus, our findings reveal the novel role of SET in fine-tuning the phosphorylation level at the kinetochore by balancing the activities of Aurora B and PP2A.

scholarly journals VX-680 Inhibits Aurora A and Aurora B Kinase Activity in Human Cells

Cell Cycle ◽  
2007 ◽  
Vol 6 (22) ◽  
pp. 2846-2854 ◽  
Author(s):  
Rebecca K. Tyler ◽  
Natalia Shpiro ◽  
Rodolfo Marquez ◽  
Patrick A. Eyers
Keyword(s):  
Kinase Activity ◽  
Human Cells ◽  
Aurora B ◽  
Aurora A ◽  
Aurora B Kinase

The dietary flavonoid luteolin inhibits Aurora B kinase activity and blocks proliferation of cancer cells

2012 ◽  
Vol 46 (5) ◽  
pp. 388-396 ◽  
Author(s):  
Fang Xie ◽  
Qingyu Lang ◽  
Mei Zhou ◽  
Haoxing Zhang ◽  
Zhishun Zhang ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Kinase Activity ◽  
Aurora B ◽  
Aurora B Kinase ◽  
Dietary Flavonoid

scholarly journals Use of DT40 conditional-knockout cell lines to study chromosomal passenger protein function

2010 ◽  
Vol 38 (6) ◽  
pp. 1655-1659 ◽  
Author(s):  
Xavier Fant ◽  
Kumiko Samejima ◽  
Ana Carvalho ◽  
Hiromi Ogawa ◽  
Zhenjie Xu ◽  
...  
Keyword(s):  
Cell Lines ◽  
Protein Function ◽  
Kinase Activity ◽  
Current Knowledge ◽  
Conditional Knockout ◽  
Aurora B ◽  
Aurora B Kinase ◽  
Chromosomal Passenger ◽  
Passenger Protein

The CPC [chromosomal passenger complex; INCENP (inner centromere protein), Aurora B kinase, survivin and borealin] is implicated in many mitotic processes. In the present paper we describe how we generated DT40 conditional-knockout cell lines for incenp1 and survivin1 to better understand the role of these CPC subunits in the control of Aurora B kinase activity. These lines enabled us to reassess current knowledge of survivin function and to show that INCENP acts as a rheostat for Aurora B activity.

scholarly journals Bub1 overexpression induces aneuploidy and tumor formation through Aurora B kinase hyperactivation

2011 ◽  
Vol 193 (6) ◽  
pp. 1049-1064 ◽  
Author(s):  
Robin M. Ricke ◽  
Karthik B. Jeganathan ◽  
Jan M. van Deursen
Keyword(s):  
Protein Kinase ◽  
Transgenic Mice ◽  
Chromosome Segregation ◽  
Kinase Activity ◽  
Tumor Formation ◽  
High Expression ◽  
Aurora B ◽  
Aurora B Kinase ◽  
Clinical Prognosis ◽  
Poor Clinical Prognosis

High expression of the protein kinase Bub1 has been observed in a variety of human tumors and often correlates with poor clinical prognosis, but its molecular and cellular consequences and role in tumorigenesis are unknown. Here, we demonstrate that overexpression of Bub1 in mice leads to near-diploid aneuploidies and tumor formation. We found that chromosome misalignment and lagging are the primary mitotic errors responsible for the observed aneuploidization. High Bub1 levels resulted in aberrant Bub1 kinase activity and hyperactivation of Aurora B kinase. When Aurora B activity is suppressed, pharmacologically or via BubR1 overexpression, chromosome segregation errors caused by Bub1 overexpression are largely corrected. Importantly, Bub1 transgenic mice overexpressing Bub1 developed various kinds of spontaneous tumors and showed accelerated Myc-induced lymphomagenesis. Our results establish that Bub1 has oncogenic properties and suggest that Aurora B is a critical target through which overexpressed Bub1 drives aneuploidization and tumorigenesis.

scholarly journals Gradient of Increasing Aurora B Kinase Activity Is Required for Cells to Execute Mitosis

2010 ◽  
Vol 285 (51) ◽  
pp. 40163-40170 ◽  
Author(s):  
Zhenjie Xu ◽  
Paola Vagnarelli ◽  
Hiromi Ogawa ◽  
Kumiko Samejima ◽  
William C. Earnshaw
Keyword(s):  
Kinase Activity ◽  
Aurora B ◽  
Aurora B Kinase

scholarly journals CSC-1

2003 ◽  
Vol 161 (2) ◽  
pp. 229-236 ◽  
Author(s):  
Alper Romano ◽  
Annika Guse ◽  
Ivica Krascenicova ◽  
Heinke Schnabel ◽  
Ralf Schnabel ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Genetic Analysis ◽  
Chromosome Segregation ◽  
Kinase Activity ◽  
Aurora B ◽  
Aurora B Kinase ◽  
C Elegans ◽  
The Individual

The Aurora B kinase complex is a critical regulator of chromosome segregation and cytokinesis. In Caenorhabditis elegans, AIR-2 (Aurora B) function requires ICP-1 (Incenp) and BIR-1 (Survivin). In various systems, Aurora B binds to orthologues of these proteins. Through genetic analysis, we have identified a new subunit of the Aurora B kinase complex, CSC-1. C. elegans embryos depleted of CSC-1, AIR-2, ICP-1, or BIR-1 have identical phenotypes. CSC-1, BIR-1, and ICP-1 are interdependent for their localization, and all are required for AIR-2 localization. In vitro, CSC-1 binds directly to BIR-1. The CSC-1/BIR-1 complex, but not the individual subunits, associates with ICP-1. CSC-1 associates with ICP-1, BIR-1, and AIR-2 in vivo. ICP-1 dramatically stimulates AIR-2 kinase activity. This activity is not stimulated by CSC-1/BIR-1, suggesting that these two subunits function as targeting subunits for AIR-2 kinase.

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