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R E V I E W Open Access
CP110 and its network of partners coordinately
regulate cilia assembly
William Y Tsang
1,2,3*
and Brian D Dynlacht
4
Abstract
Cilia are hair-like protrusions found at the surface of most eukaryotic cells. They can be divided into two types,
motile and non-motile. Motile cilia are found in a restricted number of cell types, are generally present in large
numbers, and beat in a coordinated fashion to generate fluid flow or locomotion. Non-motile or primary cilia, on
the other hand, are detected in many different cell types, appear once per cell, and primarily function to transmit
signals from the extracellular milieu to the cell nucleus. Defects in cilia formation, function, or maintenance are
known to cause a bewildering set of human diseases, or ciliopathies, typified by retinal degeneration, renal failure
and cystic kidneys, obesity, liver dysfunction, and neurological disorders. A common denominator between motile
and primary cilia is their structural similarity, as both types of cilia are composed of an axoneme, the ciliary
backbone that is made up of microtubules emanating from a mother centriole/basal body anchored to the cell
membrane, surrounded by a ciliary membrane continuous with the plasma membrane. This structural similarity is
indicative of a universal mechanism of cilia assembly involving a common set of molecular players and a
sophisticated, highly regulated series of molecular events. In this review, we will mainly focus on recent advances in
our understanding of the regulatory mechanisms underlying cilia assembly, with special attention paid to the
centriolar protein, CP110, its interacting partner Cep290, and the various downstream molecular players and events
leading to intraflagellar transport (IFT), a process that mediates the bidirectional movement of protein cargos along
the axoneme and that is essential for cilia formation and maintenance.
Keywords: Centrosomes, Cilia, Ciliogenesis, CP110, Cep290, BBSome, IFT, Protein network
Review
Links between cilia, centrosomes, and the cell cycle
It is well known that cilia and centrosomes share an in-
timate relationship during the cell cycle. A centrosome
consists of a pair of centrioles, termed the mother and
daughter centrioles, embedded in a poorly defined
pericentriolar matrix, from which cytoplasmic micro-
tubules emanate and grow [1-4]. The mother centriole
can be distinguished from the daughter centriole by the
presence of distal and sub-distal appendages. Distal ap-
pendages are thought to be important for the docking
of a basal body to the cell membrane and the recruit-
ment of IFT proteins prior to cilia assembly, whereas
sub-distal appendages anchor microtubules, participate
in endosome recycling, and form the basal foot, a struc-
ture essential for ciliogenesis and ciliary beating in
motile cilia [5-9]. In proliferating cells, a single centro-
some in the G1 phase undergoes duplication in the S
phase. The two centrosomes then separate, migrating
to opposite poles and establishing a bipolar spindle
in mitosis. Upon cell cycle exit, a centrosome obtains
competence for ciliogenesis, whereby the mother centriole
is converted into the basal body. Depending on the cell
type and/or cilia type, the basal body can migrate and
anchor to the cell surface or dock ciliary vesicles, which
elongate and eventually fuse with the plasma mem-
brane. In both scenarios, the basal body serves to nu-
cleate the growth of axonemal microtubules, a process
highly dependent on IFT [10-12]. IFT is bidirectional,
and this property can be explained by the existence of
biochemically and functionally distinct protein com-
plexes, IFT-B and IFT-A. While IFT-B and IFT-A are
commonly believed to direct anterograde (cell body to
* Correspondence: william.tsang@ircm.qc.ca
1
Institut de recherches cliniques de Montréal, 110 avenue des Pins Ouest,
Montréal, QC H2W 1R7, Canada
2
Faculté de Médecine, Université de Montréal, Montréal, QC H3C 3J7, Canada
Full list of author information is available at the end of the article
© 2013 Tsang and Dynlacht; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the
Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use,
distribution, and reproduction in any medium, provided the original work is properly cited.
Tsang and Dynlacht Cilia 2013, 2:9
http://www.ciliajournal.com/content/2/1/9
cilia) and retrograde (cilia to cell body) transport of mac-
romolecules, respectively, recent evidence indicates that
IFT-A is also involved in anterograde transport [13-16].
IFT is essential for cilium assembly and maintenance, since
the organelle lacks protein synthesis machinery [17]. When
cells re-enter the cell cycle, cilia are disassembled, and the
basal body relocates to the cell interior, assuming a
position near the nucleus. It is logical to postulate
that controls must exist to suppress the inappropriate
assembly of cilia in proliferating cells or the untimely
assembly of a bipolar spindle in non-proliferating
cells. In addition, vesicular trafficking, mother centri-
ole/basal body migration to the cell surface, basal
body anchoring to the cell membrane, and IFT must
be tightly regulated in a temporally-, spatially-, and
cell-type-specific manner to ensure the fidelity of
ciliogenesis. Indeed, a growing number of proteins, includ-
ing many that were originally identified in a proteomic
screen for novel centrosomal and ciliary components
[18-20], are known to modulate cilia assembly in a posi-
tive or negative manner [21,22], suggesting that cilia as-
sembly involves a complex circuitry controlled by the
coordinated inhibition of negative regulators and recruit-
ment and activation of positive regulators.
The CP110-Cep97 pathway
While there are many important modulators of cilio-
genesis, two distal centriolar proteins, CP110 and Cep97,
were the first proteins shown to negatively regulate cilia
assembly [23]. Loss of either protein elicits premature
inappropriate cilium formation in proliferating cells,
whereas its over-expression inhibits ciliogenesis in
non-proliferating cells. Fittingly, patients with chronic
rhinosinusitis, a respiratory disease associated with abnor-
mal or lack of motile cilia, have elevated levels of CP110
[24]. While the precise function of Cep97 awaits further
experimentation, this protein might serve as a chaperone
to stabilize CP110, allowing the co-recruitment of both
proteins to the centrosome. CP110, on the other hand, is
thought to impose a structural role at the centrosome and
forms discrete complexes critical for cell cycle regulation
and cilia assembly (Figure 1) [23,25-31]. This protein does
not have an associated enzymatic activity; rather, it was
shown to localize to the distal ends of centrioles, forming a
‘cap’above the growing microtubules that could restrain
microtubule growth [32]. Indeed, CP110 has the ability to
control centriole length in non-ciliated human [33-35] and
insect cells [36] and to block ciliary axoneme formation in
ciliated mammalian (RPE-1 and NIH-3T3) cells [23,25].
Paradoxically, CP110 does not modulate cilia length,
suggesting that at least in ciliated cells, CP110 could ‘switch
off’the ciliogenic program. Tellingly, CP110 is completely
extinguished from the basal body in ciliated cells (Figure 1
and [23]). The loss of CP110 effectively liberates the
mother centriole from its centrosomal role in cell division
and ‘licenses’the transition from mother centriole to basal
body. Thus, it appears that the removal of CP110 from the
mother centriole, rather than cell cycle control per se,
could play a crucial role in the initiation of ciliogenesis.
CP110 levels and localization to the centrosome are
tightly regulated in a cell cycle dependent manner [29].
CP110 protein levels drop significantly in G2/M and
G0/G1 phases as a consequence of transcriptional con-
trols, ubiquitin-mediated proteasomal destruction, and
microRNA-mediated turnover of CP110 mRNA [37-39].
Furthermore, disappearance of CP110 from the basal
body in quiescent cells coincides with an enrichment of
a serine/threonine kinase, Ttbk2, at the same location
(Figure 2) [40]. Ttbk2, a microtubule plus-end tracking
protein, likely promotes the onset of ciliogenesis by co-
operating with end binding proteins [40-42]. Depletion
of Ttbk2 impairs both the loss of CP110 and the recruit-
ment of IFT complexes, including IFT88, a protein local-
ized to the distal appendages of the emerging basal body
and/or the transition zone [40]. Further, the loss of
Cep83, a distal appendage protein that functions in a
concerted and hierarchical manner to recruit other pro-
teins (including Cep89, SCLT1, FBF1, and Cep164), pre-
vents the recruitment of Ttbk2 to, and the release of
CP110 from, the basal body, thereby blocking basal body
anchoring to the cell membrane (Figure 2) [43]. Another
study highlighted a role for CCDC41/Cep83 in the re-
cruitment of IFT20 to the basal body and ciliary vesicle
docking to the mother centriole as important functions
of CCDC41/Cep83 during early ciliogenesis, although
Cep164 localization and abundance were not substan-
tially impacted [44]. Since Cep83 and Cep164 can recruit
IFT proteins to the basal body and/or the transition
zone, these results imply that distal appendage proteins,
Ttbk2, CP110, and IFT proteins could functionally inter-
act [43,45]. In addition to Ttbk2, the loss of a second
serine/threonine kinase, MARK4, causes mis-localization
of its interacting partner, Odf2, which is normally found
at sub-distal appendages, and likewise, inhibits cilia for-
mation by preventing the removal of CP110/Cep97 from
the basal body (Figure 2) [46-48]. In light of recent find-
ings that distal and sub-distal appendages are assembled
independently of one another [43], these intriguing
observations suggest that Ttbk2 and MARK4 activities
might be necessary to modulate the molecular frame-
work of distal and sub-distal appendages, respectively,
ultimately leading to the destruction and removal of
CP110 from the basal body. Alternatively, the two kinases
could function after the assembly of the appendages to
remove CP110 [49]. Furthermore, these studies suggest
that protein phosphorylation is crucial for the maturation
of a mother centriole into a functional basal body, and
future phospho-proteomic studies, in combination with
Tsang and Dynlacht Cilia 2013, 2:9 Page 2 of 8
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high resolution imaging, will be essential to identify key
substrates and to examine these maturation events in
greater detail.
CP110-interacting partners and its protein network
Besides Cep97, CP110 has been shown to associate with
a cadre of proteins important for ciliogenesis, suggesting
that it could assemble a multi-functional platform to in-
tegrate centriolar and basal body functions (Figure 2).
Cep104, a microtubule plus-end tracking protein identi-
fied by a proteomic screen for novel end binding-
interacting partners, interacts with CP110 and Cep97
[41]. This protein co-localizes with CP110 at the distal
ends of centrioles in proliferating cells and is similarly
absent from the basal body in quiescent cells. However,
unlike CP110 and Cep97, Cep104 is essential for cilio-
genesis, suggesting that it may regulate axonemal growth
at the onset of cilia assembly by counteracting the activ-
ities of CP110 and Cep97. In contrast to Cep104, another
protein, Kif24, appears to reinforce the role of CP110 as
a suppressor of ciliogenesis [28]. As a member of the
microtubule de-polymerizing kinesin family of proteins,
Kif24 specifically de-polymerizes and remodels centriolar
microtubules at the mother centriole/basal body, and de-
pletion of this protein promotes ciliation, whereas over-
expression inhibits cilia growth. Although Kif24 binds
CP110 and Cep97, it specifically stabilizes CP110 and
recruits it to the centrosome, suggesting that both the
de-polymerizing activity of Kif24 and its ability to re-
cruit a distal end capping protein (CP110) to centrioles
contribute to cilia suppression. In addition, CP110 has
been demonstrated to associate with a human ciliopathy
protein, Cep290, (also known as BBS14, NPHP6, JBTS5,
SLSN6, MKS4 and LCA10; [25]). Its many names
can be attributed to the diverse spectrum of clinical
manifestations, including Bardet-Biedl syndrome (BBS),
nephronophthisis, Joubert syndrome, Senior-Loken
syndrome, Meckel-Gruber syndrome, and Leber con-
genital amaurosis, associated with mutations in the
Cep290 gene [50-52]. Despite the identification of over
S
G2 M
Duplication
G1
Separation
Maturation
PM
G0
Cilia
Assembly
Cep76
CP110
Neurl4
CP110
Cyclin/cdk
Mother Centriole
Chromosome
Daughter Centriole
Pro-centriole
Cilium
CP110
Cytokinesis
Over-duplication
Centrin
CP110
CaM
Cep290
CP110 Cep104
Kif24
P
Usp33
Cyclin F
PPhosphorylation
Cep97
Figure 1 The role of CP110 in cell cycle control and ciliogenesis. CP110 and its network of partners form distinct complexes that regulate
different aspects of centrosome function, including centrosome over-duplication, centrosome separation, cytokinesis, and cilia assembly. The
localization of CP110 is also illustrated. PM denotes plasma membrane.
Tsang and Dynlacht Cilia 2013, 2:9 Page 3 of 8
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100 unique mutations, there is no clear relationship be-
tween genotype and phenotype. The loss of Cep290 abol-
ishes cilia assembly and disrupts the migration/anchoring
of centrioles to the cell cortex, suggesting that this pro-
tein functions to promote ciliogenesis at an early step
of the ciliogenic pathway [21,25,53]. This positive func-
tion of Cep290 is antagonized by CP110, and over-
expression of a CP110 mutant refractory to Cep290
binding is incapable of suppressing ciliation in non-
proliferating cells. Because the protein levels of Cep290
remain constant throughout the cell cycle, including
G0 [25], it seems plausible that CP110 restrains
Cep290 activity in proliferating cells through direct
interaction, but once cells exit the cell cycle, the loss
of CP110 protein releases Cep290 from inhibition. It is
currently not clear how Cep290 might promote centri-
ole migration/anchoring to the cell cortex, although it
is known that this protein directly interacts with an-
other ciliopathy protein NPHP5 [54], and depletion of
NPHP5 phenocopies the loss of Cep290 [55-57]. Inter-
estingly, analysis of the primary amino acid sequence of
Cep290 reveals the presence of multiple N-terminal tropo-
myosin homology domains and a C-terminal myosin-tail
homology domain, suggesting that it might have an actin-
related function, and that centriole migration/anchoring
could involve cytoskeletal re-organization and modulation
of actin dynamics [51,58]. Indeed, the role of actin cyto-
skeleton dynamics in cilia assembly has recently been illus-
trated in a high-throughput RNA interference screen,
wherein actin polymerization was shown to have an inhibi-
tory role in cilia assembly [22]. Two proteins belonging to
the gelsolin family members, GSN and AVIL, promote cili-
ation by severing actin filaments. On the other hand,
ACTR3, a protein known to mediate the formation of
branched actin networks, suppresses cilia formation. Treat-
ment of cells with drugs that inhibit actin filament
polymerization and/or affect actin dynamics, such as cyto-
chalasin D or latrunculin B, can facilitate ciliation in
addition to causing an increase in cilium length [22,55].
Notably, impaired cilia formation associated with the loss
of Cep290 or NPHP5 can be restored by the aforemen-
tioned drugs, strongly suggesting that proteins involved in
the regulation of actin dynamics could influence the
ciliogenic pathway and could be exploited as potential
therapeutic targets [55]. Besides Cep290 and NPHP5, two
other ciliopathy-associated proteins, MKS1 and MKS3, are
also required for the translocation of centrioles to the cell
surface, whereas IFT88 is not [59]. Thus, it seems likely
that a subset of centrosomal proteins is specifically dedi-
cated to basal body migration and anchoring to the cell
membrane, and it will be most interesting to identify the
complete set of factors that control this important process.
Cep290 function and its protein network
Beyond its potential contribution in basal body migra-
tion and/or anchoring to the cell membrane, Cep290
has additional functions critical to cilia assembly. An ele-
gant ultra-structural study conducted in Chlamydomonas
reinhardtii suggests that Cep290 localizes to the transi-
tion zone, a small region immediately distal to the basal
body characterized by the presence of Y-shaped fibers
that connect the axonemal microtubules to the ciliary
Figure 2 A system-wide schematic of protein interaction networks that modulate cilium assembly. Solid lines indicate known
protein-protein interactions, confirmed by immunoprecipitation, yeast two-hybrid, and/or in vitro binding experiments. Not every
protein-protein interaction indicated is direct. Dashed lines indicate known functional connections with no evidence of protein-protein
interactions to date. EB denotes end binding proteins.
Tsang and Dynlacht Cilia 2013, 2:9 Page 4 of 8
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membrane [60]. This region is thought to regulate the
entry and exit of protein and lipid cargos into and out of
the ciliary compartment. Consistent with this idea,
Cep290 is present at the transition zone of rat motile tra-
cheal cilia [61] and associates with CC2D2A and TCTN1,
both of which are known to form a large protein complex
with several other ciliopathy proteins (AHI1, MKS1,
TCTN2, TCTN3, B9D1, B9D2, TMEM216, TMEM67) at
the transition zone (Figure 2 and [62-64]). Cep290 also
binds to Cep162, an axoneme-recognition protein re-
quired for transition zone assembly (Figure 2 and [65]).
In addition, Cep290 is required for the targeting of
Rab8a, a small GTPase responsible for vesicular trafficking
into the cilium in cultured human epithelial cells [25,53],
and has a functional connection with the BBSome, a stable
multi-subunit complex known to mediate ciliary transport
(Figure 2). The BBSome is composed of seven BBS pro-
teins (BBS1, BBS2, BBS4, BBS5, BBS7, BBS8, and BBS9)
and BBIP10, a protein required for cytoplasmic micro-
tubule polymerization and acetylation. Assembly of the
BBSome follows a hierarchical order that initially involves
the stabilization of BBS7 by the chaperonin complex
(MKKS/BBS6, BBS10, BBS12 and CCT/TRiC family of
chaperonins), followed by the formation of the BBSome
core (BBS7, BBS2, BBS9) and the subsequent incorpor-
ation of the remaining BBSome subunits through a series
of protein-protein interactions [66,67]. Interestingly, two
components of the BBSome, BBS4 and BBS8, are not
properly recruited to the cilium upon Cep290 loss [68].
The lack of BBSome recruitment to the cilium could be
due to an assembly defect, as Cep290 is known to directly
interact with MKKS/BBS6, a chaperonin-like molecule
required at an early step in BBSome assembly [69]. In
addition, a Cep290 mutant in Chlamydomonas reinhardtii
possesses malformed flagella with abnormal protein com-
position, with increased amounts of IFT-B proteins and
decreased amounts of IFT-A proteins, suggesting that
retrograde and possibly anterograde IFT are impaired [60].
AlthoughneitherCep290norCP110hasbeendemon-
strated to directly interact with IFT proteins thus far, a
proteomic screen reveals IFT122 as a novel interacting
partner of NPHP5 (Figure 2 and [56]), a protein that dir-
ectly binds to, and shares a number of common features
with, Cep290 [55-57]. Further experiments will be neces-
sary to delineate the extent to which the CP110-Cep290
axis overlaps with the BBSome and/or the IFT pathway.
Other than its localization to the transition zone, Cep290
is also targeted to centriolar satellites [53,58]. Centriolar
satellites are small, electron-dense proteinaceous granules
found in the vicinity of the centrosome and have been
implicated in microtubule-dependent protein trafficking
towards the centrosome [70-72]. These structures may
be closely related to the pericentrosomal pre-ciliary com-
partment reported at the basal body during the onset of
ciliogenesis [22]. Interestingly, several satellite components,
including PCM1, BBS4, OFD1, Cep72, and Cep290 are re-
quired for cilia assembly, and the integrity of these unique
structures is highly dependent on protein-protein interac-
tions between them (Figure 2) [53,68,73]. Of note, BBS4 is
unique among satellite proteins in that it completely re-
localizes from its original satellite position to the cilium
during ciliogenesis [74]. Thus, Cep290, together with other
satellite proteins, might regulate the trafficking of BBS4 be-
tween the two different sub-cellular compartments, and
henceplayanindirectroleinBBSomeassembly.Further
studies will be needed to decipher the mechanisms
through which satellite proteins (and possibly other un-
identified associated factors) modulate the number, size,
and integrity of satellites in space and time and how such
modulation contributes to basal body function, transition
zone assembly, and ciliogenesis.
The role of the BBSome and the IFT complex
BBS is a ciliopathy characterized by renal and retinal
failure, obesity, polydactyly, diabetes, hypogenitalism,
and hypertension [75]. Seventeen causative genes have
been identified so far, and recent studies have begun to un-
ravel the role of BBS proteins in cilia homeostasis. As men-
tioned earlier, eight different proteins (BBS1, BBS2, BBS4,
BBS5, BBS7, BBS8, BBS9, and BBIP10) are required to
form a functional unit called the BBSome [74,76]. Intri-
guingly, the BBSome binds Rabin8, a GDP/GTP exchange
factor for Rab8a, and directly interacts with phospholipids,
suggesting that this complex likely mediates vesicular traf-
ficking during ciliogenesis (Figure 2) [74]. More recently,
another BBS subunit, BBS3/Arl6, an Arf-like GTPase, was
shown to be a major effector of the BBSome [77]. BBS3/
Arl6 recruits the BBSome to the membrane, where it as-
sembles a ‘coat’that sorts proteins to the cilium. This ‘coat’
recognizes a unique ciliary localization signal found in sev-
eral ciliary membrane proteins, leading to their efficient
trafficking to the cilium [77,78]. Future biochemical and
biophysical studies will shed light on the structure of the
‘coat’and the precise nature of the ciliary localization signal
it recognizes.
Although the BBSome is thought to play an important
role in sorting certain membrane proteins to the cilium,
neither this complex, nor its assembly factors or BBS3/
Arl6, is generally required for ciliogenesis, as depletion
or loss of some of these proteins does not severely im-
pair ciliation but rather leads to defective IFT transport
[79-82]. In addition, while BBS knockout mice (BBS1,
BBS2, BBS4, BBS6 or BBS7) display subtle phenotypes
[81,83-86], a loss of BBS7 in combination with a reduc-
tion in IFT function results in a more severe phenotype
[85], suggesting that the BBSome and the IFT complex
could function in a synergistic manner. These find-
ings have led to the speculation that the BBSome is only
Tsang and Dynlacht Cilia 2013, 2:9 Page 5 of 8
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responsible for transporting a subset of ciliary proteins,
whereas the IFT complex is more universally required for
all transport processes. Recently, an elegant study which
combines a whole-genome mutagenesis screen for mu-
tants with abnormal cilia formation, time-lapse micros-
copy, and bimolecular fluorescence complementation in
Caenorhabditis elegans showed that the BBSome acts on
the IFT complex by controlling its assembly and turn-
around in cilia [14]. The BBSome first interacts with the
IFT complex (Figure 2) and motor proteins to organize
them into a functional super-complex. This super-
complex undergoes anterograde transport to the ciliary
tip, and once there, the BBSome dissociates from the
IFT complex, unloading cargos during the process. The
BBSome then re-organizes the IFT complex and re-
loads new cargos for retrograde transport back to the
ciliary base. It remains to be determined if the role of
the BBSome in worms is mechanistically conserved in
higher eukaryotes, since subtle differences exist in the
ciliary structures, and not every BBS subunit is evolu-
tionarily conserved. Nevertheless, elucidating the mo-
lecular functions of the individual BBS and IFT
components would undoubtedly provide a better un-
derstanding of how these two complexes coordinately
promote cilia assembly.
Conclusions
Our knowledge of the architecture of the cilium and the
functions of individual ciliary components has expanded
considerably in the past 10 to 15 years. The use of
forward and reverse genetic screens, animal models,
system-wide proteomics, time-lapse microscopy, cryo-
electron microscopy, and new innovations in super-
resolution microscopy have led to rapid and unprece-
dented breakthroughs in the field, highlighted by many
landmark discoveries. Among these, CP110 and Cep290
have emerged as key players in the regulation of the cilia
assembly process. Despite our current knowledge of
their functions, important questions remain: is CP110
the protein responsible for the conversion of mother
centrioles (ciliogenesis incompetent) to basal bodies
(ciliogenesis competent), and how are the diverse func-
tions of Cep290 intertwined, if at all, in modulating cilia
assembly? We believe that the answers to these questions
lie in our ability to decipher and build upon the existing
ciliary protein interaction network (Figure 2). These stud-
ies should allow us to understand how this network con-
tributes to health and disease and to devise rational
therapeutic approaches for treating ciliopathies based on
these proteomic and genetic networks.
Abbreviations
IFT: Intraflagellar transport; BBS: Bardet-Biedl syndrome.
Competing interests
The authors declare that they have no competing interests.
Authors’contributions
WYT wrote the manuscript. WYT and BDD revised the manuscript. Both authors
read and approved the final manuscript.
Acknowledgements
We thank Sehyun Kim for critically reading the manuscript, and we apologize to
our colleagues whose findings could not be included due to space limitations.
WYT was a Canadian Institutes of Health Research New Investigator and a Fonds
de Recherché Santé Junior 1 Research Scholar. This work was supported by the
Canadian Institutes of Health Research (MOP-115033) to WYT and by an NIH
grant (1R01HD069647-01) to BDD.
Author details
1
Institut de recherches cliniques de Montréal, 110 avenue des Pins Ouest,
Montréal, QC H2W 1R7, Canada.
2
Faculté de Médecine, Université de
Montréal, Montréal, QC H3C 3J7, Canada.
3
Division of Experimental Medicine,
McGill University, Montréal, QC H3A 1A3, Canada.
4
Department of Pathology
and Cancer Institute, Smilow Research Center, New York University School of
Medicine, New York, NY 10016, USA.
Received: 29 April 2013 Accepted: 3 July 2013
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doi:10.1186/2046-2530-2-9
Cite this article as: Tsang and Dynlacht: CP110 and its network of
partners coordinately regulate cilia assembly. Cilia 2013 2:9.
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