Review TRENDS in Plant Science
2 February 2005
Transcriptional networks in plants
MYB–bHLH–WD40 protein complex and
the evolution of cellular diversity
Nicola A. Ramsay1 and Beverley J. Glover 2
1
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK CB2 2QH
2
Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge, UK CB2 3EA
A protein complex composed of MYB and bHLH
transcription factors associated with a WD40 repeat
protein initiates multiple cellular differentiation path-
ways in a range of plants. Recent reports have provided
the first coherent models of the network of interactions
that lead to diverse cell fates through the activity of this
protein complex. The resulting flexibility in plant mor-
phology is likely to have played a major role in angio-
sperm evolution and success. The complex appears to
have arisen in the land plant lineage, although its com-
ponent parts are considerably more ancient. Here, we
review the evolutionary history of the MYB–bHLH–WD40
protein complex and its role in generating plant epi-
dermal cellular diversity.
Introduction
The transition from unicellularity to multicellularity
necessitated cellular specialization via increased cellular
diversity. To achieve cellular diversity and to ensure
correct temporal and spatial cellular distribution, signals
– both external environmental and internal cellular
stimuli – must be integrated and subsequent regulation
of gene expression must be coordinated. Genes encoding
proteins that generate and receive signals have broad
effects on plant development and the consequences of
mutations are likely to be wide ranging and possibly
deleterious. Similarly, coding regions of structural genes
with key developmental roles are highly conserved and
are therefore rarely a source of developmental diversity.
However, transcription factors and their DNA binding
sequences, which lie in the cis regulatory elements of their
target genes, are of central importance to the generation of
phenotypic variation. Because transcription factors act in
concert with other regulators, the same transcription
factor can be used repeatedly, with the outcome of the
DNA binding event determined by which other regulators
act in concert or opposition. Here, we consider the function
of a complex of transcription factors that can include
various members of the MYB, basic helix–loop–helix
(bHLH) and WD40 protein families. Recent reports have
provided insight into how this one complex regulates
multiple cell fates and has therefore played a key role in
the evolution of cellular diversity in the plant epidermis.
Corresponding author: Glover, B.J. (bjg26@cam.ac.uk).
Available online 6 January 2005
www.sciencedirect.com 1360-1385/$ - see front matter Q 2005 Elsevier Ltd. All rights reserved. doi:10.1016/j.tplants.2004.12.011
Vol.10 No.
Plant epidermis as a system to investigate cellular
diversity
The plant epidermis is the first point of contact between the
sessile plant and its changing environment. As such, the
epidermis fulfils several distinct roles and this multi-
functionality makes it an ideal system for the study of
evolution of morphological diversity. The plant epidermis
primarily provides an impermeable barrier to water,
allowing organisms that evolved in the sea to survive in a
dehydrating terrestrial atmosphere. Concurrently, the
epidermis of vascular plants adapted to allow carbon dioxide
to enter as effectively as if an epidermis were absent, an
improvement over more basal plant groups, whose pores are
unable to respond to changing atmospheric conditions. The
secondary functions adopted by the epidermis are variable.
Box 1 details the functions of the different epidermal cell
types whose specification is discussed below.
A common regulatory complex regulates epidermal
cell fate
A common set of proteins interact to form a regulatory
complex that controls epidermal cell identity and ensures
appropriate spatial and temporal distribution of special-
ized epidermal cells. The individual components of this
complex are discussed in more detail below.
WD40 repeat proteins
WD40 repeat proteins comprise a family in the b-propeller
protein group, which is characterized by the presence of a
40 residue core region delineated by a glycine–histidine
(GH) dipeptide and a tryptophan–aspartate (WD) dipep-
tide [1]. This motif is tandemly repeated four to 16 times
in the same protein. The most extensively studied WD40
repeat protein is the Gb subunit of heterotrimeric
G proteins involved in signal transduction, which forms
a seven-bladed b-propeller structure containing seven
WD40 repeats. In addition to signal transduction, these
proteins are involved in many functions and, given this
functional diversity, it is unsurprising that there is little
sequence similarity between family members. A common
function of WD40 repeat units is that they facilitate
protein–protein interactions and have no intrinsic enzym-
atic function. Several WD40 repeat containing proteins
that affect epidermal traits have been identified from
petunia (AN11; see Glossary), Arabidopsis (TTG1), Perilla
(PFWD) and maize (PAC1; Table 1). These proteins belong
64 Review TRENDS in Plant Science
Box 1. Functions of specialized plant epidermal cells
Structure and spacing
Pavement cells (Figure Ic, scale barZ50 mm) are the most common
epidermal cell type and are morphologically unspecialized, providing
mechanical strength while being sufficiently pliable to allow growth.
Pavement cells protect subsidiary cell layers and ensure appropriate
spacing of morphologically and functionally more specialized epi-
dermal cell types.
Regulation of water loss and gaseous exchange
Stomata (Figure Ib, scale barZ50 mm) are necessary for water reten-
tion while allowing the gaseous exchange essential for photosyn-
thesis [45]. Stomatal spacing is non-random and partially cell lineage
dependent. The pattern of stomatal initials is modified by interactions
between developing complexes, interactions between stomata and
other epidermal cells and environmental inputs [46].
Nutrient uptake
Root hairs (Figure Id, scale barZ20 mm) are unicellular tip-growing
structures that increase the root surface area for nutrient and water
uptake. Arabidopsis root hair development is controlled by positional
cues, with root hairs located over the join of adjacent cortical cells
beneath [47]. The cell-to-cell communication required for root hair cell
fate determination begins during embryo development, with posi-
tional information from underlying cell layers breaking the initial
symmetry of root epidermal hair files and establishing a pattern over
which cellular differentiation is determined [23,46].
(a)
(b) (d)
(c)
Figure I.
to the same clade and could form a surface on which other
proteins interact [2–5]. Ectopic expression of the non-
Arabidopsis WD40 proteins in a ttg1 mutant background
complements several of the Arabidopsis mutant pheno-
types, suggesting that they can interact with similar
protein partners (Table 1). Genetic analyses and yeast
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Vol.10 No.2 February 2005
Protection against predation
At their simplest, trichomes (Figure Ie, scale barZ50 mm; reproduced,
with permission, from Ref. [48]) provide a physical barrier against
herbivore attack. More complex trichomes protect the plant by
poisoning insects with secretions [49]. They have also been suggested
to reduce transpiration and to protect against ultraviolet radiation. The
presence of pigments (Figure Ia, scale barZ1.5 cm) and other second-
ary metabolites could further protect the epidermis by decreasing its
palatability [49]. The Arabidopsis trichome is a single cell with three
branches and a set of distinct socket cells around the base [50].
Trichomes differentiate while the surrounding epidermal cells are still
dividing and their distribution on the Arabidopsis leaf is not random.
At the time of initiation, trichome cells are separated by an average
of three intervening cells, a separation that cannot at this stage be
attributed to a cell lineage based mechanism [50].
Attraction of pollinators
Epidermal cells can be specialized to attract pollinators by the pro-
duction of colourful pigments (Figure Ia; [51]), the release of scent [52]
or the adoption of specialized conical shapes (Figure If) that enhance
aspects of light and heat capture [53]. It is also possible that petal
epidermal cell shape could be used by bees as a tactile cue in flower
discrimination or to enhance scent volatilization [53].
(e)
(f)
two-hybrid experiments have identified these partners as
belonging to the bHLH and MYB classes of proteins [6–8].
bHLH proteins
bHLH family members have a basic helix–loop–helix
domain that was initially identified in the animal
 Review TRENDS in Plant Science Vol.10 No.2 February 2005 65

maize tissue-specific anthocyanin pigmentation and was

Glossary
the first plant bHLH protein to be isolated [12]. Mutant
AN1: Anthocyanin1. analyses have identified additional plant bHLH proteins
AN2: Anthocyanin2.
AN11: Anthocyanin11. involved in anthocyanin biosynthesis (Table 1). These pro-
C1: Colorless 1. teins show substantial amino acid conservation throughout
CPC: Caprice. the protein. Overexpression of Lc in an Arabidopsis ttg1
EGL3: Enhancer of Glabra3.
ETC1: Enhancer of TRY and CPC 1. mutant background complements phenotypes besides lack
FLP: Four Lips. of anthocyanins, indicating the involvement of bHLH
GL1: Glabrous1. proteins with similarity to Lc in other aspects of epidermal
GL3: Glabra3.
Lc: Leaf color. cell fate [13]. Consistent with this observation, several
PAC1: Pale Aleurone Color1. Lc-like proteins have been shown to affect traits in addition
PAP1: Production of Anthocyanin Pigment 1.
to anthocyanin biosynthesis (Table 1).
PAP2: Production of Anthocyanin Pigment 2.
PFWD: Perilla frutescens WD. Lc functions in conjunction with a member of the
TRY: Triptychon. MYB class of transcription factors to activate anthocyanin
TT2: Transparent Testa2.
TT8: Transparent Testa8.
expression in maize [14]. This is a common theme in other
TTG1: Transparent Testa Glabra1. plant species, in which an Lc-like bHLH protein requires
WER: Werewolf. a MYB protein partner to function [6–8,15,16]. In addi-
tion, several Lc-like proteins interact directly with the
Arabidopsis WD40 repeat protein TTG1 [6–8].
transcriptional regulators MyoD and Myc [9]. The basic
region of the bHLH domain is responsible for sequence-
specific DNA binding to a consensus hexanucleotide MYB proteins
E-box, CANNTG [10], whereas the HLH region allows Plant MYB proteins are transcriptional regulators that
homo- and heterodimer formation [11]. Lc is involved in are characterized by either two (R2 and R3) or three

Table 1. bHLH, MYB and WD40 repeat proteins identified as being involved in the control of epidermal cell fate identity by mutant or
ectopic expression analysis (indicated by a coloured bar)

a
Ectopic expression of maize Lc in an Arabidopsis ttg1-1 mutant background was able to complement the trichome, anthocyanin pigmentation, root hair, seed coat
pigmentation and seed coat mucilage defects [12].
b
AN1 also affects vacuolar pH and seed coat cell shape in Petunia [25].
c
Ectopic expression of GL1 and WER under the control of the cis regulatory sequences of the other demonstrated that the proteins are functionally interchangeable [20].
d
Ectopic expression of MIXTA in tobacco resulted in the production of multicellular trichomes and conical cells on leaves [64].
e
MIXTA controls the formation of conical petal cells in Antirrhinum [63].
f
Ectopic expression of the maize PAC1 gene in an Arabidopsis ttg1 null mutant background was able to complement the trichome, anthocyanin pigmentation, seed coat
pigmentation and seed coat mucilage defects [2].
g
Ectopic expression of PFWD in Arabidopsis caused the formation of supernumerary trichomes and elevated anthocyanin levels [7].
h
L.B. Lai et al., unpublished.

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66 Review TRENDS in Plant Science Vol.10 No.2 February 2005

(R1, R2 and R3) imperfect repeats of the MYB DNA-
binding motif [17,18]. Most plant MYB proteins belong to
the R2R3 family, and C1 (a regulator of maize anthocyanin
production) is the founding member [19]. R2R3 MYB
proteins control anthocyanin biosynthesis in species other
than maize and MYB proteins have been identified that
affect other aspects of epidermal cell fate (Table 1). All
show considerable sequence divergence outside of the
MYB motif, even those with identical function between
species. In spite of this lack of obvious sequence similarity
outside of the MYB domains, maize C1 and petunia AN2
(both controlling anthocyanin biosynthesis) are function-
ally interchangeable [20]. More surprisingly, GL1 and
WER [R2R3 MYB proteins involved in specifying different
epidermal cell fates in Arabidopsis (root and trichome
production, respectively) and exhibiting only 23% sequence
identity at their C-termini] are also functionally equiva-
lent when placed under the control of the other’s
regulatory sequences [21]. Many of these MYBs have
been shown to interact with Lc-like bHLH proteins and a
WD40 repeat protein [6–8]. In Arabidopsis, proteins
containing a single MYB repeat and lacking a transactiva-
tion domain have been identified and found to be involved
in specifying aspects of epidermal cell fate [22–24]. These
proteins interact with TTG1 and an Lc-like bHLH protein,
and, owing to the lack of a transcriptional activation
domain, form an inactive complex [25,26].
How can a transcription complex with three
components control such diverse aspects of epidermal
cell fate?
The transcription complex composed of a WD40, a bHLH
and a MYB protein regulates the expression of multiple
distinct target genes in a range of plant species. Insights
into how this complex influences epidermal cell identity
were provided by studies of Arabidopsis mutants. In
Arabidopsis, the WD40 repeat protein TTG1 is central to
all aspects of epidermal cell fate, positively regulating
trichome formation, anthocyanin production, seed-coat
pigmentation and seed-coat mucilage production, and
negatively regulating hypocotyl stomatal-cell identity
and root-hair formation (perhaps by initiating the differ-
entiation of alternative cell fates) (Table 1; Figure 1)
[3,27]. TTG1 provides a scaffold allowing protein–protein
interactions between the bHLH and MYB proteins, thus
explaining the pleiotropic effect of ttg1 mutations.
On the basis of transgenic experiments, it was
hypothesized that a bHLH protein with sequence simi-
larity to maize R was involved in epidermal cell fate
determination [13]. The cloning of GL3 (from Arabidopsis)
and the subsequent identification of the similar genes TT8
and EGL3 verified this [7,8]. Recent work has shown that
these proteins all interact with TTG1 and affect overlap-
ping subsets of the cell fate pathways that TTG1 regulates
(Figure 1) [6–8]. Association of GL3 with TTG1 regulates

Trichome
initiation
lls nt

N a tyl
st po lls
ce me

on ta
om co
hy ce
ve

- l
Pa

YB

R2R3 MYB
R2
M

R3
le
ng

M
Si

YB

bHLH
coat pigment
R2R3 MYB

R2R3 MYB
Non-root
hair cell

Seed
files

WD40
bHL
LH

H
bH

R
2R
3

YB
M
YB

M
le
An

ng R2R3 MYB
th

Si
oc
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ha s

a
e

ni
ir
oo fil

ns
R ell
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Seed coat
mucilage
TRENDS in Plant Science

Figure 1. Interactions between WD40, bHLH and MYB transcription factors in Arabidopsis resulting in different epidermal cell types. In Arabidopsis, TTG1 (a WD40 repeat
protein) is involved in specifying all epidermal cell types in concert with the bHLH proteins GL3, EGL3 or TT8, which exhibit a high degree of amino acid sequence similarity. In
turn, the bHLH proteins interact with either R2R3 MYB repeat proteins (which are highly divergent from one another and specific for individual epidermal cell fates) or single
MYB repeat proteins, which are more similar to one another and result in an inactive transcription complex.

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 Review TRENDS in Plant Science
trichome, root-hair and anthocyanin production; EGL3
regulates the same three pathways and also that leading
to the production of seed-coat mucilage; TT8 interacts
with TTG1 to specify only synthesis of anthocyanin, seed-
coat mucilage and seed-coat pigmentation [7,8,28]. In
turn, the bHLH proteins interact with MYB proteins that
exhibit specificity for individual developmental pathways
within these subsets (Table 1) [6–8,28]. The combinatorial
interaction of these proteins influences epidermal cell
identity and it is the R2R3 MYB proteins that ultimately
determine which cell fate is adopted. By contrast, the
single-repeat MYB proteins TRY, CPC and ETC1, which
lack transcriptional activation domains, are partially
redundant and might prevent the formation of a func-
tional WD40–bHLH–MYB complex by competing with
R2R3 MYB proteins for bHLH proteins [22,24–26].
The requirement for a WD40–bHLH–MYB transcrip-
tion complex has been established for the control of antho-
cyanin biosynthesis in other plant species [29]. Heterologous
expression of these proteins from other species in
Arabidopsis mutant backgrounds has demonstrated
their ability to complement mutations that perturb
aspects of epidermal cell fate beside anthocyanin biosyn-
thesis. However, this potential to participate in diverse
aspects of epidermal cell fate is not always evident in the
endogenous system. The petunia protein AN1 is the only
such protein, apart from those of Arabidopsis, that has
been shown to affect cell fate decisions besides antho-
cyanin synthesis [29]. The control of other aspects of
epidermal cell fate in other plant species might differ from
that in Arabidopsis, with only anthocyanin biosynthesis
conserved, or there might be as yet unidentified ortho-
logues of the Arabidopsis genes.
Evolutionary history of the MYB–bHLH–WD40
activation complex
The WD40 repeat proteins form an ancient family that is
found in all eukaryote genomes analysed. They have been
reported from animals (including bilaterians and the
cnidarian Hydra vulgaris), fungi and the slime mould
Dictyostelium, as well as from plants [30]. Their ubiqui-
tous nature suggests that they are ancestral to the modern
eukaryotes, but they are present in few non-eukaryotic
genomes: only in Anabaena, Synechocystis and Thermo-
monospora (http://bmerc-www.bu.edu/wdrepeat/). The
absence of WD40 repeat proteins from E. coli and other
bacterial genomes, as well as from archaeal genomes,
suggests that they were acquired by an ancestral
eukaryote from a cyanobacterial relative (such as the
a-proteobacteria, proposed ancestors of mitochondria
[31]). In all proteins studied, WD domains act as sites for
interactions with other proteins, but the range of proteins
with which they interact is large and varies between
kingdoms. Many animal genomes have experienced more
extensive duplications of the family than seen in plant
genomes, adding to the diversity of their roles [30].
The bHLH proteins are probably descended from
prokaryotic transcription factors containing a helix–
loop–helix structure. In eukaryotes, HLH domains are
associated with a basic domain at their N-terminal side,
which is necessary for DNA recognition and binding.
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Vol.10 No.2 February 2005 67
These bHLH proteins evolved early in the eukaryotic
lineage [32] and are present in plants, animals and fungi
[33]. The bHLH proteins are DNA-binding proteins found
in all eukaryotic lineages. Their numbers are limited in
animals but their roles are usually essential [32]; in plants,
their repeated duplication has generated enormous fami-
lies, often with overlapping or redundant roles [33].
The MYB gene family is eukaryote specific [34] and has
followed divergent evolutionary pathways in plants and
animals. In animals, a limited number of duplications of a
gene encoding three MYB repeats gave rise to a small gene
family; by contrast, in plants, multiple duplications of both
a three-repeat MYB and MYB genes encoding only one
or two MYB repeats gave rise to an extensive and varied
family [35]. Evolutionary debate has centred on whether
these divergent evolutionary histories indicate polyphyle-
tic origins of MYB proteins within animal and plant
lineages [34,36]. However, the identification of both two-
repeat and three-repeat MYB proteins in the ciliate
Sterkiella histriomuscorum suggests strongly that the
evolutionary origins of the MYB family lie in the uni-
cellular eukaryotes [37]. In all systems analysed, MYB
proteins are DNA binding and might activate or repress
transcription through interactions of their C-terminal
regions with other components of the eukaryotic tran-
scriptional machinery [38].
In animal systems, there are no data indicating that
animal MYB and bHLH proteins act together with a
WD40 repeat protein, but vertebrate c-Myc has been
shown to have a possible c-Myb-activating function [39].
The complex as it forms in plants controls epidermal
phenotype in several higher plants, and can thus be
estimated to be at least 120 million years old.
Recruitment of the complex within the land
plant lineage
Because the components of the MYB–bHLH–WD40 com-
plex were present in the ancestors of all plants and
because modern angiosperms use the whole complex, we
must search for its first usage as a complex in older plant
lineages. There is currently little known about the roles of
these proteins in any plant more basal than the gymno-
sperms, but a potential member of the complex (PpMYB1)
has been described in the moss Physcomitrella patens [40].
PpMYB1 shows sequence similarity to AmMIXTA, which
modifies the activity of a bHLH protein in a heterologous
host (B. Glover and C. Martin, unpublished). Further
work in this system should elucidate the early role of the
complex in land plants. Evidence that it could be func-
tional in the gymnosperm lineage has emerged recently
from work focusing on the MYB component. A gene was
isolated from Picea mariana (black spruce) that shows
sequence similarity to maize C1. In concert with the maize
R gene (encoding a bHLH protein), this new sequence was
sufficient to induce activity of the promoter of the maize
Bronze2 gene (which encodes an enzyme in the antho-
cyanin biosynthetic pathway) in cell cultures [41]. The
demonstration that a gymnosperm MYB protein can
substitute for a maize MYB protein in the maize complex
suggests strongly that the protein complex is active
in gymnosperms. Further work in this system should
68 Review TRENDS in Plant Science
clarify the sequences and functions of the bHLH and
WD40 components.
Once adopted by land plants, the MYB–bHLH–WD40
complex was recruited to control the diversity of epidermal
cell development. This single regulatory complex has been
used so extensively by plants because of its simplicity,
flexibility and plasticity. It is a clear example of evolution-
ary and genetic thriftiness, with an established network
of tried and tested regulatory motifs being co-opted to
produce new phenotypic traits by variation of the bHLH
or, more usually, the MYB component. Regulatory genes
and their own regulatory sequences, as well as their target
DNA-binding sequences, are able to evolve more rapidly
than the structural genes they control [42]. DNA-binding
sequences have even greater flexibility than coding regions
because cis regulatory sequences are modular, allowing
each module to act and evolve independently. This results
in greater heterozygosity (and hence variability) in the
regulatory sequences than there is in the coding sequences
[42]. The combination of the flexibility inherent in the
MYB–bHLH–WD40 complex and the variability of the
regulatory DNA to which it binds has resulted in a system
so flexible that it is responsible for generating most of the
diversity of plant epidermal cells.
The flexibility of this complex, and particularly the
MYB component, will allow continued modification in
response to changing pressures on epidermal cell deve-
lopment in the future. Indeed, recent evidence has emerged
that the MYB component of the complex is still evolving
in maize, in which a new allele has been described from a
maize line indigenous to the Bolivian highlands [43]. The
pl-bol3 allele contains three copies of the pl1 gene with
different regulatory regions. The proteins encoded by this
allele interact with a unique set of bHLH proteins and
result in a novel pattern of anthocyanin deposition, which
could provide a selective advantage by protecting under-
ground organs from predation and limiting damage from
ultraviolet light [43].
Constraints on the evolution of the system
The structural integrity of the individual protein com-
ponents of the MYB–bHLH–WD40 complex is determined
by interactions that occur between their constitutive
amino acids. This restricts the amino acid changes that
can occur. In particular, maintenance of the seven-bladed
b-propeller structure of the WD40 repeat protein places
exquisite constraints on the extent to which this protein
can evolve [1]. The requirement to interact with other
protein components for functional activity places addi-
tional limitations on the evolution of all components of the
MYB–bHLH–WD40 protein complex. Recent yeast-two-
hybrid analyses [6–8] have demonstrated that the bHLH
component interacts with both the WD40 repeat and the
MYB components of the complex, and can also homo-
dimerize or heterodimerize with related bHLH proteins.
These multiple protein–protein interactions impose con-
straints on the variability of the bHLH because mutation
of the domains involved in these interactions could affect
the structure and function of the whole complex. By
contrast, the MYB protein only interacts with the bHLH
partner, partially explaining why the bHLH has been less
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Vol.10 No.2 February 2005
free to evolve than the MYB partner. Finally, the regions of
both bHLH and MYB proteins responsible for DNA bind-
ing must remain highly conserved to achieve sequence
specificity, limiting the extent to which variation is possible.
Conclusions
The recruitment of a MYB protein, a bHLH protein and
a WD40 repeat protein into a single complex appears to
have occurred only in the plant lineage. Following dupli-
cation and mutation of the genes encoding the different
components of this complex, particularly the MYB com-
ponent, the whole complex acquired the flexibility to
specify multiple cell fates, providing the developmental
machinery necessary to generate the diversity of cell types
present in the plant epidermis. Our understanding of the
function of this complex in Arabidopsis is now almost
complete and we can trace the evolutionary history of
its individual components back to ancestral unicellular
eukaryotes. A fuller understanding of the evolution of
plant epidermal cell diversity requires us to link dupli-
cations of MYB-, bHLH- and WD40-encoding genes with
the appearance of particular cell types in the fossil record.
Similar work with the genes encoding MADS box proteins
has produced a picture of morphological evolution tied to
the duplication and diversification of particular genes in
the family [44]. To paint a similar picture explaining the
evolution of cellular diversity within the angiosperms will
require future work to focus on the isolation and functional
characterization of members of the MYB–bHLH–WD40
complex in more ancestral plant groups, and, in particu-
lar, on the interactions of members of the complex with one
another. It is likely that many more genes encoding MYB
proteins will be identified than genes encoding bHLH
and WD40 proteins, and one challenge will be to identify
the subset of these that operate in a bHLH- and WD40-
containing protein complex. Once the members of these
complexes have been isolated and their interactions
defined, it should be possible to detect co-evolution by
analysing sequence evolution at the sites of interaction.
Given the importance of flexible development and a multi-
functional epidermis to the success of the angiosperms,
this work will be important in explaining a major part of
the molecular evolution that gave rise to their great diversity.
Acknowledgements
We thank Kit Wilkins and John Runions for Figure Ie. We also thank the
BBSRC and the Royal Society for financial support.
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