Journal of Cell and Molecular Biology 10(2):1-10, 2012
Haliç University, Printed in Turkey.
http://jcmb.halic.edu.tr
Review Article 1
Transforming acidic coiled-coil proteins and spindle assembly
Seema TRIVEDI*
(* author for correspondence; [email protected])
Received: 2 January 2012; Accepted: 5 November 2012
Abstract
Transforming acidic coiled-coil proteins (TACC) are essential for mitosis not only by their association
with the centrosome and assembly of spindle microtubules, but also by involvement in cell cycle
checkpoints. In order to stabilize spindle fibers, TACCs interact with other microtubule-associated
proteins (MAPs). Dysregulation of TACCs may lead to abnormal cell division that may result in
chromosomal abnormality or tumorigenesis. This review focuses on facts known so far regarding
TACC proteins, their interactions and their involvement in spindle microtubule stability in higher
eukaryotes.
Keywords: Cancer, microtubules, centrosome, spindle fibers, transforming acidic coiled-coil proteins
Özet
Dönüştürücü asidik sarmalanmış sarmal proteinleri ve iğ iplikçiğinin birleşmesi
Dönüştürücü asidik sarmalanmış sarmal proteinleri (TACC) sadece sentrozomlarla ve iğ iplikçiği
mikrotübülleriyle birleşmesiyle olan ilişkileri açısından değil, ayrıca hücre döngüsü kontrol
noktalarına dahil olmaları açısından da mitoz için gereklidir. İğ iplikçiklerini stabilize etmek amacıyla,
TACC’ler diğer mikrotübül ilişkili proteinlerle (MAP) etkileşime girer. TACC’lerin yanlış
düzenlenmesi kromozomal anormallikler ya da tümörigenez ile sonuçlanan anormal hücre
bölünmelerine neden olabilir. Bu derleme, bugüne kadar TACC proteinleri, etkileşimleri ve yüksek
ökaryotlarda iğ iplikçiği kararlılığına katkıları ile ilgili bilinen gerçekler üzerinde durmaktadır.
Anahtar Kelimeler: Kanser, Mikrotübüller, Sentrozom, İğ iplikçikleri, Dönüştürücü asidik
sarmalanmış sarmal proteinleri
Abbreviations
TACC = Transforming Acidic Coiled-coil, MAP = Microtubule Associated Protein, Msps = Mini
spindles, MT = Microtubule, ch-TOG = Colonic–hepatic Tumour-Overexpressed Gene, AAK =
Aurora A Kinase
Introduction
Transforming acidic coiled-coil protein (TACC) is
a family of the microtubule associated proteins
(MAPs) that is crucial for spindle assembly,
maintaining bipolarity and microtubule (MT)
stability during mitosis (Still et al., 2004; Brittle
and Ohkura, 2005; Pearson et al., 2005). TACCs
are even important in acentrosomal (acentriolar or
anastral) meiosis in females of many animal
species where spindle formation is
chromosome centric (Pearson et al., 2005).
TACCs do not have microtubule
stabilizing activity on their own. Instead,
they form complexes with other MAPs to
stabilize spindle fibers. TACC/MAP
complex provides stable association of MTs
with centrosomes at the minus end (Albee
and Wiese, 2008) possibly after release from
2 Seema TRIVEDI
the nucleation site from kinetochores (reviewed in
Raff, 2002). The complex associates at the plus
ends of the MTs growing out from the centrosome
during nucleation (reviewed in Raff, 2002).
However, the exact mechanism by which TACC
interacts with other MAPs and recruits them to the
centrosome is not clearly understood. In
Drosophila, D-TACC recruits Mini spindles protein
(Msps; a conserved family of MAP) (reviewed in
Raff, 2002) and in Xenopus, maskin (TACC3) form
a complex with XMAP215 (Albee and Wiese,
2008). However, the XMAP215 complex may
associate with both plus and minus ends of the MT.
Similarly, human TACCs and ch-TOG (colonic–
hepatic tumour-overexpressed gene) (homologue of
Msps) possibly form a structural lattice at
centrosomes to maintain the integrity of spindle
poles and to stabilize spindle MTs (reviewed in
Raff, 2002; Gergely et al., 2003). However, it is not
known why in cultured human cells TACC3 and, in
Drosophila D-TACC, these proteins are apparently
not essential for recruitment of XMAP215 analogue
(Brittle and Ohkura, 2005). This review focuses on
genomic locations, protein characteristics and
interactions of TACC proteins in humans and
general aspects of role of TACC proteins in spindle
dynamics in higher eukaryotes.
TACC genes and proteins
Three TACC proteins have been identified in
humans, namely TACC1, 2 and 3. The three human
TACCs are related by ~200-amino-acid C-terminal
region (the ‘TACC domain’), which is predicted to
form a coiled coil domain (reviewed in Raff, 2002).
Besides TACC domain, these proteins share
homology (except Drosophila D-TACC) in the
SDP domain as well (Lauffart et al., 2002; Still et
al., 2004). SDP domain is composed of functionally
conserved repeats of 33 amino acids, though the
numbers of repeats are different in different TACC
proteins. Interaction of SDP domain with
transcription factor GAS41/NuBI1 (also known as
YEATS4) has been established (Lauffart et al.,
2002) but this interaction possibly does not directly
affect spindle formation.
Genomic locations of human TACC
reference gene sequences as per NCBI and
details of proteins obtained from SwissProt
are given in Table 1.
Though implicated in several cancers, no
mutations have been reported in the TACC1
gene (Still et al., 2008). TACC1 mRNA
exon 3 contains a predicted nuclear
localization signal (Still et al., 2008), shows
ubiquitous expression and encodes a
cytoplasmic protein which is mainly
perinuclear protein (molecular mass of 125
kDa) (Conte et al., 2002) but different
isoforms in different cells may be localized
in the cytoplasm as well (Lauffart et al.,
2006).
TACC1 protein does not show
compositional bias whereas TACC2 has
poly-lysine and poly-proline rich regions
and TACC3 has poly-serine regions (Table
1). In addition, different sites in the TACC
proteins show post translational covalent
modifications (Table 2). Phosphotyrosine is
seen only in TACC1, while N6-acetyl lysine
is
seen
only
in
TACC3
and
phosphothreonine is not seen in TACC1. It
is also pertinent to note that TACC1
phosphorylation varies in different isoforms
(Still et al., 2008).
TACC2 concentration at the centrosome
has been observed even during interphase
unlike TACC1 and TACC3 proteins
(Gergley et al., 2000a). TACC3, also known
as ERIC1 (Still et al., 2004; Eslinger et al.,
2009) a non-motor MAP, was also identified
as an ARNT interacting protein (Aint1) in
mice (Aitola et al., 2003) and is expressed in
proliferative tissues (Aitola et al., 2003;
reviewed in Hood and Royle, 2011). During
mitosis, TACC3 is localized to centrosome
but during interphase, TACC3 is seen in
cytoplasmic or perinuclear regions (Piekorz
et al., 2002). The TACC3 gene has five
reported mutations: CAG to CGG, TCG to
TTG, CGT to TGT, CAG to TAG and TCA
to TTA (Eslinger et al., 2009).
TACC proteins in spindles 3
Table 1. Human TACC Genomic Location (as per NCBI+), Introns, mRNA And Splice Variants (as per NCBI AceView+)
and Protein Details (as per SwissProt*).
Official Symbol
Genomic Location
TACC1
8p11.22
TACC2
10q26
TACC3
4p16.3
Genomic Sequence
NC_000008.10
38585704..38710546
NC_000010.10
123748689..124014057
NC_000004.11
1723266..1746898
Number of Introns+
44
49
23
mRNA+
38 (7 unspliced)
35 (7 unspliced)
16 (3 unspliced)
Protein*
TACC1 (O75410
TACC1_HUMAN)
805
TACC2 (O95359
TACC2_HUMAN)
2948
TACC3 (Q9Y6A5
TACC3_HUMAN)
838
Length (number of amino acids)
Number of Isoforms+
27
Features
Description
Coiled coil
Potential
TACC1
610 - 805
26
15
Position
TACC2
TACC3
2675 - 2703
637 - 837
2746 - 2947
2420 - 2423
Poly-Lys
Compositional
bias
155 - 160
Poly-Ser
Pro-rich
1956 - 2016
SPAZ
2315 - 2403
482 - 549
Domain
Motif
SPAZ 1
215 - 297
SPAZ 2
Bipartite
nuclear
localization
signal 1
Potential
Bipartite
nuclear
localization
signal 2
Potential
359 - 507
Interaction
with CH-TOG
226 - 241
455 - 471
701 - 805
Interaction
with LSM7
and SNRPG
1 - 55
Interaction
with TDRD7
152 - 259
Interaction
with YEATS4
206 - 427
Region
+
Thierry-Mieg and Thierry-Mieg 2006, AceView-Dec 2009
4 Seema TRIVEDI
Table 2. Modification types and positions of modifications in TACC proteins as per SwissProt.*
N6-acetyl
Protein Position
Phosphoserine Phosphothreonine Phosphotyrosine
lysine
TACC1
TACC2
TACC3
44
50
52
54
55
57
228
276
406
533
197
201
493
571
575
758
962
1025
1267
1313
1426
1562
1946
1949
2072
2073
2226
2246
2256
2317
2321
2359
2389
2390
2392
2394
2403
2512
2884
25
59
71
175
317
434
558
*Grey cells indicate presence and blank cells indicate absence or not known.
Spindle assembly and TACC proteins
TACC proteins interact with MTs (particularly at
the minus end) and are mainly associated with
centrosome (Gergely et al., 2000a and 2000b). The
distribution and concentrations of TACC proteins
during
spindle
formation
vary.
TACC1
concentration at centrosome is weak and is seen
only during mitosis. TACC2 concentration is strong
at centrosome throughout the cell cycle. TACC3 is
strongly concentrated in a more diffused region
around
centrosomes (during G2 phase) at the minus
end of spindle MTs (Gergely et al., 2000a;
Gergely et al., 2000b; Barr et al., 2010).
Once the spindle has formed, TACC3
protein is not found at astral MTs (reviewed
in Raff, 2002; Hood and Royle, 2011).
TACC3 protein is localized at centrosomes
with γ-tubulin and spindle MTs with αtubulin (Piekorz et al., 2002, reviewed in
(Raff, 2002; Hood and Royle, 2011),
particularly during S, G2 and M phases of
cell cycle (Piekorz et al., 2002). TACC3/ch-
TACC proteins in spindles 5
TOG/clathrin complex increases the stability of Kfibers during early mitosis. This is achieved by
reduction in MT catastrophe by anchoring to the
spindle and establishing short bridges. Involvement
of TACC proteins in formation of long bridges is
not known but possibly HURP and the kinesinrelated protein HSET/KIFC1 may be involved in
longer bridges (Booth et al., 2011).
TACC3 depleted cells do not show proper
metaphase alignment; therefore it is possible that
TACC3 protein may be essential for chromosome
alignment (Gregely et al., 2003). TACC3 may also
affect early mitotic checkpoint by associating with
pS939-TSC2 (tuberous sclerosis complex 2) and
regulating its localization at spindle poles and also
possibly affect nuclear envelope (Gomez-Baldo et
al., 2010). TACC3 affects spindle checkpoint by
affecting SAC (spindle assembly checkpoint
assembly) by stabilizing spindle and is important
for microtubule-kinetochore interaction. Depletion
of TACC3 results in activation of the SAC (spindle
assembly checkpoint protein), which prevents
degradation of cyclin B1 and anaphase transition.
Cyclin B1 is present in cells from late G2 to
metaphase and is degraded prior to anaphase.
TACC3 depletion increases the levels of cyclin B1
but not cyclin A (S/G2) (Schneider et al., 2007),
thus presence of TACC3 would affect degradation
of cyclin B1 and help in anaphase transition.
These observations indicate differences in roles
of different types of TACC proteins during mitosis.
For proper assembly and stability of spindle
fibers and minus end of centrosome associate MT,
phosphorylation of TACC is essential which is
mediated by mitotic kinases (e.g. Aurora A kinase
i.e. AAK) (Barros et al., 2005, Peset et al., 2005).
Absence of phosphorylated TACC may result in
either shorter centrosomal MT or absence of these
spindle fibers (Peset et al., 2005, Kinoshita et al.,
2005). Phosphorylation occurs at different sites in
different animals. In Xenopus TACC3/Maskin, at
least two residues (main site is Ser626) are
phosphorylated; in Drosophila D-TACC Ser863 is
phosphorylated exclusively at centrosomes and in
human Ser558 is phosphorylated in TACC3
(reviewed in Raff, 2002; Brittle and Ohkura, 2005;
LeRoy et al., 2007). Phosphorylation of TACCs
may also help G2/M checkpoint by proper
microtubule assembly, thus the control of mitosis
by affecting G2/M transition (Conte et al., 2002;
reviewed in Bettencourt-Dias and Glover, 2007),
particularly
via
spindle
checkpoint
(Schneider et al., 2007).
However, AAK itself must be activated
prior to being able to phosphorylate the
TACC proteins. In humans, AAK is
activated by binding with TPX2 [Targeting
Protein for Xklp2 (Xenopus plus enddirected kinesin-like protein)]. AAK-TPX2
binding is activated by HURP (Human
hepatoma up-regulated protein) which is a
MAP protein that can also bind directly to
MTs. However, HURP itself needs
activation by Ran (RAs-related Nuclear
protein) (Sato et al., 2009; Sato and Toda,
2010).
On the other hand, dephosphorylation of
TACC proteins may also affect spindle
stability. In this regard, Mars (a D.
melanogaster sequence homologue of
HURP) mediates spatially controlled
dephosphorylation of TACC for spindle
stability, perhaps only at the centrosome.
Dephosphorylated TACC establishes lateral
interactions with MT or with plus ends
which may be impaired due to TACC
phosphorylation at Ser863 (Tan et al.,
2008).
Spindle fibers and proteins interacting
with TACC proteins
Minimal interactions of TACCs with other
proteins or ligands were determined using
the STRING web interface (Jensen et al.,
2009), and are shown in Figure1. As
previously stated, TACC1 and TACC3 bind
with ch-TOG (clathrin, colonic and hepatic
tumor overexpressed gene) (Conte et al.,
2002; Lauffart et al., 2002); however, from
the interaction shown in Figure 1 it appears
that all three TACC proteins interact with
CKAP5 (homologue XMAP215 or chTOG). The other two common interactions
of the three TACC proteins are YEATS4
(also called YAF9; GAS41; NUBI-1)
(transcription factor, protein located in
nucleoli) and LSM7 (a conserved subfamily
of Sm-like small proteins). LSM7 associates
with U6 snRNPs and plays a role in several
aspects of mRNA processing (Conte et al.,
2002; Lauffart et al., 2002).
6 Seema TRIVEDI
TACC1 may also be involved in gene regulation by
affecting mRNA translation by interaction with
TDRD7 (tudor domain containing 7) (Figure 1).
TDRD7 protein is a part of cytoplasmic RNA
granules involved in mRNA regulation. It is not
known whether the involvement of TACCs in RNA
processing or interaction with transcription factors
has any role in MT dynamics during cell division.
As per Figure 1, TACC1 and 3 also interact
with AURKB and AURKA. These two proteins
also interact with Cyclin B1 (which controls entry
in mitosis) (Conte et al., 2002). Studies have shown
that TACC3 is involved in localization of the
mitotic kinase Aurora B and the checkpoint protein
BubR1 at kinetochores thus affecting MT
attachment (Schneider et al., 2007).
TACC2 protein also directly interacts with
SMYD2 (SET- and MYND-containing protein 2)
(Figure 1). SMYD2 activates TACC2 gene by
methylation of H3K4 in the promoter region of
TACC2 gene besides the involvement of SMYD2
in some protein-protein interactions. These protein
interactions may have roles in centrosomal MT
formation (Abu-Farha et al., 2008) but apparently
not by directly interacting with TACC2 protein.
Phosphorylated TACC3 also directly interacts
with clathrin heavy chain (CLTC) that promotes
accumulation of other complex members at the
mitotic spindle (reviewed in Hood and Royle,
2011). Another direct interaction of TACC3 protein
with septin-7 (SEPT7, CDC10 protein homolog) is
shown in Figure 1. SEPT7 associates with the
mitotic spindle and the kinetochore. It has also been
shown that SEPT7 is needed for stable localization
of CENP-E (centromere-associated protein E) at
kinetochore besides affecting spindle checkpoint
(Zhu et al., 2008). Association of SEPT7 and
MAPs, particularly MAP4, in MT dynamics both
during interphase and mitosis has been established
(Silverman-Gavrila et al., 2008), and it is possible
that similar interaction of SEPT7 with TACC
proteins may affect MT stability.
Expression of TACC3 is high in hematopoietic
tissue unlike TACC1 and TACC2. Apparently
higher levels of TACC3 proteins are not for
proliferation of tissue but for direct or indirect
regulation of p53 levels to prevent apoptosis
although not true for other tissue (Piekorz et al.,
2002). Other study confirmed direct interaction of
TACC3 with p53 (that is also concentrated at
centrosomes) possibly to keep it inactive during
mitosis (reviewed in Raff, 2002) (not seen in
Figure 1).
TACC3 is necessary for proper
localization of phosphorylated TSC2
(Tuberous sclerosis proteins, tuberin) to the
mitotic apparatus and cytokinetic structures.
This interaction may be through the TSC2HBD domain (TSC2 hamartin-binding
domain) and result in promotion of
cytoskeletal remodeling (Gómez-Baldó et
al., 2010).
Though little is known about the factors
that control or regulate length of spindle
fibers, TACC3 may be one of the proteins
that control length of MTs and time for
chromosome alignment at metaphase plate
(reviewed in Raff, 2002). AAK may also
regulate MT length, as seen in Drosophila
embryos, where AAK function disturbance
leads to abnormal shortening of centrosomal
MTs. This disturbance also leads to
inefficient concentration of D-TACC at
centrosomes (reviewed in Raff, 2002).
TACCs dysregulation and cancer
Human TACC 1, 2 and 3 are present in
genomic regions that are rearranged in
certain cancer cells (reviewed in Raff, 2002;
Stewart et al., 2004; Still et al., 1999).
Aberrations of TACC genes (TACC3 in
particular)
contribute
to
tumorigenesis/cancer (reviewed in Raff,
2002; Lauffart et al., 2005).
Since TACC proteins are also involved
in centrosomal dynamics, cell cycle
checkpoints (Schneider et al., 2007) and can
form multiple complexes, any dysregulation
in these proteins may be important during
tumorigenesis (Lauffart et al., 2002). It has
been noted that increase or decrease in
levels of the TACCs can lead to impairment
of spindle functions (reviewed in Raff,
2002). Disruption of spindle function can
then lead to misalignment of chromosomes
and or abnormalities in chromosome
separation. Altered levels of TACC proteins
can lead to abnormal mitosis although next
p53 dependent checkpoint should eliminate
such cells. However, if there is simultaneous
alteration in TACC levels and p53 is either
absent or depleted, then such cells would not
TACC proteins in spindles 7
Figure 1. Predicted functional partnes (minimum interaction) of the three TACC proteins (as per
STRING Jensen et al., 1999)
undergo elimination, resulting in genetic instability
that could contribute to the development of cancer
(reviewed in Raff, 2002).
Some studies show that TACC3 may enhance
stability of tumors. This can be achieved by
TACC3 and ch-TOG in clustering of multipolar
spindles in tumor cells into two poles that may lead
to somewhat ‘normal’ division (reviewed in Hood
and Royle, 2011). However, TACC2 may be a
potential tumour suppressor (reviewed in Raff,
2002) contrary to studies that suggest no role of
TACC2 in tumor suppression (Schuendeln et al.,
2004).
Unanswered questions
Though much is known regarding TACC function
in spindle and microtubule dynamics, there are few
aspects that still remain unknown. These are
summarized below:
Roles of TACCs in regulation/control of
spindle fiber lengths are not fully
understood. Though the levels of TACC and
particularly roles of TACC3 and AAK are
indicated in control of MT length (reviewed
in Raff, 2002), the precise mechanism by
which this is achieved is not known.
Though TACC proteins are present in
cytoplasm during interphase, their fate at the
end of mitosis is not known with respect to
their redistribution to cytoplasm of the
daughter
cells.
If
there
is
exclusion/reduction in amount of TACC
proteins from nucleoplasm, the mechanism
remains elusive. Further, it is not known
whether destruction/recycling/decrease in
8 Seema TRIVEDI
expression of all TACCs (like cyclins) is important
for ending anaphase.
It is known that TACC3 associates with
kinetochore MTs (K fibers), but association with
interpolar MTs (reviewed in Hood and Royle,
2011) or astral MTs is not confirmed. It is also not
known whether all three TACCs associate with
kinetochore MTs (K fibers), interpolar MTs and
astral MTs or there are different TACC for each
fiber type.
If different TACCs are involved in K-fibers,
interpolar and astral MTs; it is not known how this
association difference is achieved.
Different interaction partners at different
subcellular locations of each splice variant of
TACC1 protein have been reported during different
stages of embryonic development. This may be
possible due to retention of coiled coil domain in
each splice variant but there are differences in
interaction motifs at N-terminus (Lauffart et al.,
2006). However, it is not known whether different
isoforms of TACC proteins have different roles in
spindle assembly during mitosis.
Conclusion
It is known that TACCs are important in
maintaining bipolarity and stability of spindle fibers
through
their
association
with
other
binding/interacting partners. TACCs also play a
role in cell cycle checkpoints due to their
association with centrosomes and p53. However,
there are many unresolved functional and structural
aspects of the three TACC proteins. Further
advancement in studies with respect to the unsolved
facets of these proteins may help in enhancing basic
understanding of spindle MT dynamics and related
disorders.
Acknowledgements
I am extremely indebted to Prof. S. D. Kapoor,
former Head, Department of English, JN Vyas
University, Jodhpur (Raj.) and Emeritus Fellow of
UGC (University Grants Commission) of India, for
correcting the language and expression in the
manuscript.
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