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Gene Section
Review
AURKB (aurora kinase B)
Sai-Ching Jim Yeung
The University of Texas M. D. Anderson Cancer Center, Department of General Internal Medicine,
Ambulatory Treatment and Emergency Care, Department of Endocrine Neoplasia and Hormonal
Disorders, 1515 Holcombe Boulevard, Unit 1468, Houston, Texas 77230-1402, USA (SCJY)
Published in Atlas Database: March 2014
Online updated version : http://AtlasGeneticsOncology.org/Genes/AURKBID731ch17p13.html
DOI: 10.4267/2042/54365
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 France Licence.
© 2014 Atlas of Genetics and Cytogenetics in Oncology and Haematology
Abstract
Location: 17p13.1
Review on AURKB, with data on DNA/RNA, on
the protein encoded and where the gene is
implicated.
DNA/RNA
Identity
Aurora kinases are conserved during eukaryotic
evolution. While the genomes of yeasts encode only
one Aurora kinase (Ipl1 in budding yeast and Ark1
in fission yeast), higher eukaryotes express two or
more members of this family. In mammals, there
are three members (Aurora A, B and C).
Description
Other names: AIK2, AIM-1, AIM1, ARK2, AurB,
IPL1, PPP1R48, STK12, STK5, aurkb-sv1, aurkbsv2
HGNC (Hugo): AURKB
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AURKB (aurora kinase B)
Yeung SCJ
Schematic diagram of protein domains of Aurora B kinase and some key facts. DN -K106R marks the location of amino acid K at
position 106 (ATP binding site), which will produce a dominant negative protein when K is mutated to R. T at position 232 is the
phosphorylation site involved in autocatalysis. The A-Box and D-Box are consensus sequences for targeted polyubiquitination
(King et al., 1996; Pfleger and Kirschner, 2000), and the A-Box in Aurora B is important for Aurora B degradation (Nguyen et al.,
2005).
Aurora A (Aurora 2, ARK1, and BTAK) is present
among all vertebrates. Aurora B (Aurora 1, ARK2,
and AIM1) and Aurora-C (Aurora 3 and AIK3)
came into existence from gene duplication during
the evolution of mammals (Brown et al., 2004).
AURKB, and the interaction with INCENP will be
affected.
In contrast, the α-helix domain for interacting with
INCENP is intact in AURKB-Sv2, but AURKBSv2 is missing major parts of the kinase domain.
Thus, AURKB-Sv2 does not have kinase activity
and may act as a dominant negative competitor
against AURKB.
Small molecule inhibitors target the ATP-binding
pocket of aurora kinases.
There are data available from the Protein Data Bank
website (http://www.pdg.org) regarding the
interaction of Aurora B with 3 inhibitors [AD6 (4[(5-bromo-1,3-thiazol-2-yl)
amino]-Nmethylbenzamide): PDB ID 2vgp (Andersen et al.,
2008), ZM447439: PDB ID 2vrx (Girdler et al.,
2008), and hesperadin: PDB ID 2bfy (Sessa et al.,
2005)].
Protein
Description
Size: 344 amino acids; molecular weight: 39.3 kDa.
The AURKB gene has 8 exons, but there are 4
isoforms of AURKB protein due to alternative
splicing.
The molecular structure of Aurora B has been
determined by crystallography (Sessa et al., 2005;
Andersen et al., 2008; Girdler et al., 2008). When
the amino acid sequences of the ATP-binding
pockets of Aurora A, B and C are compared, 3 of
the 26 residues lining the active site in Aurora A,
Leu215, Thr217 and R220, are different from the
corresponding residues in Aurora B and C (Brown
et al., 2004); there is no difference in these 26
residues between Aurora B and C. The manner in
which Aurora A binds to ATP (Bayliss et al., 2003)
and ADP (Nowakowski et al., 2002) have been
modeled. Because of the high degree of
conservation of the active site between Aurora A
and B, Aurora B is expected to interact with ATP
and ADP in the same way as reported for Aurora A.
INCENP interacts with AURKB at an α-helix
domain and activates AURKB. AURKB-Sv1 lacks
the INCENP interaction domain because part of
exon 5 is missing and intron 5 and intron 6 may
form a new domain. Therefore, the conformation of
AURKB-Sv1 is expected to be different from
Atlas Genet Cytogenet Oncol Haematol. 2014; 18(12)
Expression
The expression of Aurora kinases varies with cell
cycle phases, being at very low levels in the non-M
phases (Fu et al., 2007; Gautschi et al., 2008;
Mountzios et al., 2008).
Although Aurora A and Aurora B are
phylogenetically related, they have different
biological functions and distinct temporo-spatial
subcellular localization in mammals.
In prophase, Aurora A is at the centrosomes while
Aurora B starts to appear in the nucleus (Carmena
and Earnshaw, 2003).
In metaphase, Aurora A is near the spindle poles on
the microtubules ends while Aurora B is on the
centromeric regions of chromosomes as a
chromosomal passenger protein.
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AURKB (aurora kinase B)
Yeung SCJ
AURKB has 4 alternative splicing variants: the longest one (344 aa); AURKB-Sv1 (312 aa), which loses part of exon 5 but
contains a fragment of intron 5 and intron 6 instead; AURKB-Sv2 (303 aa), which lacks exon 6; and the shortest form (142 aa),
which loses more than the C-terminal half of the protein (López-Saavedra and Herrera, 2010). The serines and threonines are
highlighted to demonstrate the alignment. Helix domains are highlighted in magenta. The active site is highlighted in red. The
nucleotide binding region is indicated by the rectangle.
The surface model of ZM447439 bound to Aurora B (amino acid 77-361) is rendered using the program PyMOL. ZM447439 (in
stick molecular structure) is shown in the active site ATP-binding pocket of Aurora B (blue), and the 3 residues that differ
between Aurora B and A are highlighted in cyan. INCENP-A (amino acid 798-840) in complex with Aurora B is hidden by coloring
it black.
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AURKB (aurora kinase B)
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serine/threonine phosphatase type 1 (PP1) or type
2A (PP2A) (Sugiyama et al., 2002) regulate Aurora
B kinase activation while MKlp2 controls Aurora B
localization in anaphase (Gruneberg et al., 2004).
Regarding mitotic chromosome condensation,
Aurora B directly phosphorylates histone H3, not
only at S10 but also at S28. The level of S28
phosphorylation is rendered undetectable by PP1
just prior to entry into mitosis (Goto et al., 2002).
Aurora B binds three other chromosome passenger
proteins - inner centromere protein (INCENP),
Survivin and Borealin - to form a complex that
targets Aurora B to both centromeres and the
spindle. The assembly of the outer kinetochore,
which binds microtubules to control chromosome
movement, is restricted to mitosis, whereas the
inner kinetochore remains tethered to the
centromeres throughout the cell cycle. Aurora B
and PP1 coordinate and mediate cell cycledependent changes in kinetochore assembly by
regulating the phosphorylation status of kinetochore
substrates (Emanuele et al., 2008). The binding of
mitotic checkpoint kinase Budding Uninhibited by
Benzimidazoles1 beta (BubR1) to kinetochores is
regulated by the survivin/Aurora B complex.
Aurora B phosphorylates mitotic centromereassociated kinesin (MCAK) at merotelic
attachments and regulates the microtubule
depolymerase activity of MCAK (Knowlton et al.,
2006). These functions of Aurora B are essential for
proper chromosome segregation (Lens and
Medema, 2003). Aurora B regulates the cleavage
furrow-specific vimentin by phosphorylation and
controls vimentin filament segregation in
cytokinesis (Goto et al., 2003).
Checkpoint kinase 1 (Chk1) is a component of the
DNA damage checkpoint, and it augments spindle
checkpoint signaling by activating Aurora B and
BubR1 (Zachos et al., 2007). Aurora B kinase
activity is also regulated by poly(ADPribosyl)ation; activation of Poly [ADP-ribose]
polymerase 1 (PARP1) in response to DNA damage
will lead to a striking inhibition of Aurora B kinase
activity by poly(ADP-ribosyl)ation (Monaco et al.,
2005).
In anaphase, Aurora A is at the polar microtubules
while Aurora B relocates from the centromeres to
the spindle midzone (spindle equator) where the
microtubules from opposite poles interdigitate
(Keen and Taylor, 2004). In cytokinesis, Aurora B
accumulates at the cleavage furrow before finally
concentrating at the midbody.
Localisation
The protein level and kinase activity of Aurora B
are tightly controlled according to the phase of the
cell cycle and the stages in mitosis. It expression
peaks at the G2-M transition, whereas its kinase
activity and subcellular localization change quickly
according to the stage of mitosis. In mitosis, Aurora
B, Survivin, Borealin and INCENP form the
chromosomal passenger complex (Knauer et al.,
2007). It is located at the chromosomes in prophase,
the centromeres in prometaphase and metaphase,
the central mitotic spindle in anaphase, and the
cleavage furrow in cytokinesis (Adams et al.,
2001). Analysis of the dynamics of Aurora B
showed that the association of Aurora B with
centromeres is dynamic (Murata-Hori et al., 2002)
but the association with spindle microtubules
during anaphase is static. Aurora B is transported to
the equatorial cell cortex by astral microtubules.
Function
In mitosis, the chromosomal passenger complex,
composed of Aurora B, Survivin, Borealin and
INCENP, controls chromosome alignment, histone
modification, and cytokinesis (Knauer et al., 2007).
Presence of this complex at the right place at the
right time is the key to precise control of its
enzymatic core, i.e., the Aurora B kinase (Vader et
al., 2006). Although Aurora B Kinase is found in
complexes that contain Borealin, it is not required
for the mitotic phosphorylation of Borealin (Kaur et
al., 2007). Thus far, there are a number of known
substrates of Aurora B: the RNA methyltransferase
NSUN2 (Sakita-Suto et al., 2007), Septin-1 (Qi et
al., 2005), vimentin (Goto et al., 2003), histone H3
(Sugiyama et al., 2002), MgcRacGAP (Minoshima
et al., 2003), INCENP (Bishop and Schumacher,
2002; Honda et al., 2003), Survivin (Wheatley et
al., 2007) and TP53 (Gully et al., 2012).
Aurora B activity is regulated in a variety of ways.
It autophosphorylates at T232 through interaction
with INCENP (Yasui et al., 2004). The
phosphorylation of T232 is indispensable for its
kinase activity. The temporo-spatial dynamics of
Aurora B is determined by its binding to tubulin
(Warner et al., 2006), regulation by other kinases
and phosphatases (Sugiyama et al., 2002;
Gruneberg et al., 2004), and proteasomal
degradation after poly-ubiquitination (Nguyen et
al., 2005; Stewart and Fang, 2005; Sumara et al.,
2007). Survivin (Chen et al., 2003) and protein
Atlas Genet Cytogenet Oncol Haematol. 2014; 18(12)
Homology
Intriguingly, replacing the amino acid residue G198
of Aurora A with the equivalent residue N142 of
Aurora B, i.e., Aurora A (G198N), makes this
single amino acid mutant behave like Aurora B (Fu
et al., 2009). Aurora A (G198N) is localized in the
inner centromere in metaphase and the midzone in
anaphase just like Aurora B, and it can compensate
for the loss of Aurora B in chromosome
misalignment and premature exit from mitosis. It
binds to and phosphorylates INCENP and Survivin.
Therefore, the presence of glycine (G) or
asparagines (N) at a single site assigns Aurora A-
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AURKB (aurora kinase B)
Yeung SCJ
like or B-like functions and properties (Fu et al.,
2009).
Yasen et al. (Yasen et al., 2009) studied the
expression of the isoforms of Aurora B in 10 HCC
cell lines and 253 samples from patients with
varying degrees of HCC malignancy.
AURKB was aberrantly expressed in HCC cell
lines and primary HCC tumors.
Abnormal protein
Expression of AURKB-Sv2 is associated with
advanced stages of HCC, high levels of αfetoprotein, tumor invasion, multiple tumor
formation, and shortened disease-free survival
(Yasen et al., 2009).
AURKB-Sv2 may be a marker of poor prognosis.
Oncogenesis
Cell cycle phase-inappropriate phosphorylation of
histone H3 in the entire cell cycle may enhance
proliferation of liver cancer cells (Sistayanarain et
al., 2006).
Implicated in
Lung adenocarcinoma
Note
(Smith et al., 2005; Vischioni et al., 2006)
Prognosis
High Aurora B expression predicts short survival
for lung adenocarcinoma (Vischioni et al., 2006).
Oncogenesis
High Aurora B expression correlates with cell
proliferation, dedifferentiation, and metastasis in
lung cancer patients (Vischioni et al., 2006).
Acute myeloid leukemia
Note
(Ikezoe et al., 2007)
Oncogenesis
In an analysis comparing 44 samples of freshly
isolated AML cells with 11 bone marrow
mononuclear cells from healthy volunteers and 12
peripheral blood mononuclear cells from healthy
volunteers, measurement of relative mRNA
expression of Aurora B shows that it is upregulated
in the majority of cases (Ikezoe et al., 2007). In
high-risk myelodysplastic syndrome and secondary
AML, surviving and aurora B are expressed in high
levels in the CD34+ cells (Yoshida et al., 2012).
Aurora B overexpression may have contributed to
genomic instability and progression from
myelodysplastic syndrome to AML.
Glioblastoma multiforme
Note
(Zeng et al., 2007)
Prognosis
High Aurora B expression predicts short survival
for glioblastoma multiforme (Zeng et al., 2007).
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This article should be referenced as such:
Mountzios G, Terpos E, Dimopoulos MA. Aurora kinases
as targets for cancer therapy. Cancer Treat Rev. 2008
Apr;34(2):175-82
Atlas Genet Cytogenet Oncol Haematol. 2014; 18(12)
Yeung SCJ. AURKB (aurora kinase B). Atlas Genet
Cytogenet Oncol Haematol. 2014; 18(12):872-878.
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