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J Biol Chem, Vol. 274, Issue 26, 18145-18148, June 25, 1999
From the Departments of The contribution of desmosomes to epidermal
integrity is evident in the inherited blistering disorder associated
with the absence of a functional gene for plakophilin-1. To define the function of plakophilin-1 in desmosome assembly, interactions among the
desmosomal cadherins, desmoplakin, and the armadillo family members
plakoglobin and plakophilin-1 were examined. In transient expression
assays, plakophilin-1 formed complexes with a desmoplakin
amino-terminal domain and enhanced its recruitment to cell-cell
borders; this recruitment was not dependent on the equimolar expression
of desmosomal cadherins. In contrast to desmoplakin-plakoglobin interactions, the interaction between desmoplakin and plakophilin-1 was
not mediated by the armadillo repeat domain of plakophilin-1 but by the
non-armadillo head domain, as assessed by yeast two-hybrid and
recruitment assays. We propose a model whereby plakoglobin serves as a
linker between the cadherins and desmoplakin, whereas plakophilin-1
enhances lateral interactions between desmoplakin molecules. This model
suggests that epidermal lesions in patients lacking plakophilin-1 are a
consequence of the loss of integrity resulting from a decrease in
binding sites for desmoplakin and intermediate filaments at desmosomes.
Desmosomes are intercellular adhesive junctions that act as
anchorage points for intermediate filament networks. The desmosomal cadherins, desmogleins and desmocollins, bind directly to the cytoplasmic protein plakoglobin (1-3), a member of the armadillo gene
family that includes the adherens junction protein The disruption of desmosomes by gene ablation in experimental model
systems (6, 11-13) or by autoimmune antibodies in human patients (14)
severely compromises tissue integrity and function. Recently, the first
human genetic disorders involving mutations in desmosomal genes have
been reported. Haploinsufficiency of desmoplakin results in the
disruption of intermediate filament interactions with desmosomes in
palmoplantar epidermis (15). In addition, mutation of both alleles of
plakophilin-1 (PKP-1)1 and
consequent loss of the protein causes epidermal fragility, perturbed
desmoplakin localization, and detachment of intermediate filaments from
the plasma membrane of keratinocytes (16). PKP-1 was originally
identified as Band 6, a 75-kDa keratin-associated protein component of
desmosomes in stratified tissues (17). PKP-1 is also part of the
armadillo gene family (18-22). In overlay assays, PKP-1 was recently
found to bind to a number of desmosomal components, including
desmoplakin and intermediate filament polypeptides (10). However, the
mechanism by which PKP-1 contributes to desmosome assembly and
attachment to intermediate filaments remains unknown.
We report here that the non-armadillo head domain of PKP-1 binds
directly to the amino-terminal domain of desmoplakin and enhances its
recruitment to cell junctions. Our data indicate that PKP-1 is a
desmoplakin-binding partner in the desmosomal plaque and suggest a
model by which PKP-1 recruits desmoplakin to desmosomes by increasing
lateral interactions between junction components.
Cell Culture and Immunofluorescence--
COS 7 cells (subclone
20) were transiently transfected and processed for immunofluorescence
analysis as described (8, 23). To enhance detection of full-length
PKP-1 and the PKP-1 head domain, cells were permeabilized with 0.01%
saponin before fixation in methanol (24). DP-NTP was detected using the
monoclonal antibody M2 directed against the FLAG epitope tag (Eastman
Kodak Co., Rochester, NY). Rabbit polyclonal antibodies against
recombinant PKP-1 head (Ab 667) and repeat domains (Ab
670)2 were used to detect the
PKP-1 fragments.
cDNA Expression Constructs--
A cDNA encoding the
first 584 amino acids of desmoplakin (DP-NTP), and an amino-terminally
FLAG epitope-tagged version driven by the CMV promoter were described
previously (5, 8, 25). DP-NTP with a carboxyl-terminal FLAG tag was
generated by PCR, cloned into pBluescript and sequenced, and then
subcloned into the CMV expression vector. Full-length, Myc-tagged
plakoglobin and Dsg1 were described previously (8), and the full-length "a" form of PKP-1 was assembled and cloned into pCMV-Script
(Stratagene, La Jolla, CA) (19). Plasmids encoding the PKP-1 head and
armadillo repeat domains were generated by reverse transcription-PCR
using RNA isolated from A431 cells. The resulting cDNAs were
sequenced and subcloned into the pCMV5 vector (26) using the
BamHI and HindIII restriction sites. The PKP-1
head domain comprises amino acids 1-286 (ending with QVYQL) and the
repeat domain begins at amino acid 287 (GGICK).
Co-immunoprecipitation and Immunoblot
Analysis--
Co-immunoprecipitation was carried out as described
previously (8, 23). Monoclonal antibody M2 coupled to agarose beads (Kodak) was used to capture FLAG epitope-tagged DP-NTP. Antibodies to
plakoglobin (mouse mAb 11E4) (27) and PKP-1 (rabbit polyclonal Ab 667)
were used to precipitate these armadillo proteins and associated
polypeptides. Immune complexes were released by incubation in reducing
SDS-polyacrylamide gel electrophoresis sample buffer at 95 °C and
analyzed by immunoblot using Enhanced Chemiluminescence (Amersham
Pharmacia Biotech). Plakoglobin was detected using mAb 11E4, DP-NTP was
detected using a rabbit polyclonal antibody NW161 (5), and desmoglein
(Dsg1) was monitored using mAb 9E10 directed against the Myc tag
(28).
Yeast Two-hybrid Constructs and Assays--
DP-NTP in pACTII was
generated as described previously (8). The desmocollin 2a (Dsc2a)
cytoplasmic tail in pACTII was generated by PCR to include nucleotides
2198-2743 (nucleotide numbering according to Ref. 29). The PKP-1
constructs described above were subcloned into the DNA-binding domain
vector pBD-Gal4 (Stratagene) using EcoRI and SalI
restriction sites. The Dsg1 cytoplasmic domain encoding amino acids
568-1049 (MICC ... QYSK) was amplified by PCR and cloned into the
pGAD 424 vector (CLONTECH). The clone contains a
single amino acid exchange (amino acids Glu625 PKP-1 Enhances Desmoplakin Recruitment to Intercellular
Junctions--
To determine the molecular basis of the cutaneous
lesions exhibited by patients lacking PKP-1, the role of PKP-1 in
desmosome assembly was addressed by transiently expressing junctional
proteins in COS cells. We previously demonstrated that a polypeptide
comprising the first 584 amino acids of desmoplakin (DP-NTP) is
recruited to cell borders when co-expressed with a cadherin and
plakoglobin (8, 23). Here, DP-NTP was expressed alone (Fig.
1, A and B) or in
combination with full-length PKP-1 (Fig. 1, C and
D). When expressed alone, DP-NTP remained in large
cytoplasmic aggregates and exhibited minimal cell border localization
(Fig. 1A). In the presence of PKP-1, extensive DP-NTP
recruitment to intercellular junctions was observed (Fig.
1C), and PKP-1 and DP-NTP co-localized at cell borders (Fig.
1D). Nuclear staining was also observed for PKP-1,
consistent with a report that PKP-1 is present in the nucleus in many
cell types (24).
To define which domain of PKP-1 was responsible for enhancing DP-NTP
recruitment to borders, DP-NTP was co-expressed with either the head
domain of PKP-1 (Fig. 1, E and F) or with the carboxyl-terminal armadillo repeat region of PKP-1 (Fig. 1,
G and H). Similar to full-length PKP-1, the PKP-1
head domain localized at borders and in the nucleus (Fig.
1F). The head domain also enhanced DP-NTP recruitment to
borders, although to a lesser extent than full-length PKP-1. Both
full-length PKP-1 and the head domain localized to cell-cell borders
even when expressed in the absence of DP-NTP or exogenously expressed
cadherins (not shown). The PKP-1 armadillo domain did not enhance
DP-NTP recruitment to borders, and both DP-NTP (Fig. 1G) and
the PKP-1 armadillo domain exhibited a cytoplasmic distribution. These
data indicate that PKP-1 enhances DP-NTP recruitment to cell borders
and that this activity is contained within the amino-terminal head
domain of PKP-1. Furthermore, this activity does not require
co-expression of exogenous desmosomal cadherins.
PKP-1 Co-immunoprecipitates with DP-NTP and the PKP-1 Head Domain
Binds to the Amino-terminal Domain of Desmoplakin--
To establish
the hierarchy of protein-protein interactions in which PKP-1
participates, we addressed first whether PKP-1, like plakoglobin,
interacts with desmosomal cadherins and second whether PKP-1 interacts
with the amino-terminal domain of desmoplakin. PKP-1 was co-expressed
in COS cells with the desmosomal cadherin Dsg1 (Fig.
2) or with DP-NTP (Fig.
3). As reported previously (27, 30), Dsg1
and plakoglobin form complexes as demonstrated by the presence of Dsg1
in the plakoglobin immunoprecipitation (Fig. 2A). In contrast,
Dsg1 was not detected when PKP-1 was immunoprecipitated in parallel
experiments (Fig. 2B). Furthermore, PKP-1 did not co-immunoprecipitate with Dsg1 when antibodies directed against the
Dsg1 extracellular domain were used (not shown). Similar results were
obtained when Dsc2a was tested for complex formation with PKP-1 (not
shown).
Similar to previous results with plakoglobin, PKP-1
co-immunoprecipitated with DP-NTP (Fig. 3). To determine whether PKP-1 binds directly to DP-NTP or to the desmosomal cadherins, yeast two-hybrid analysis was carried out. The PKP-1 head domain and armadillo domains were tested for interactions with DP-NTP, the Dsg1
cytoplasmic domain, and the Dsc2a cytoplasmic domain. Consistent with
the co-immunoprecipitation analysis, the PKP-1 head domain interacted
strongly with DP-NTP as determined by a The results presented here provide insights into both the
molecular basis of a cutaneous disorder in patients lacking PKP-1 (16)
and into the role of PKP-1 in desmosome assembly. In addition to
binding to keratins (10, 17, 19), PKP-1 may also facilitate intermediate filament attachment to the desmosomal plaque by enhancing desmoplakin recruitment to the desmosome. In patients lacking PKP-1,
epidermal fragility and blistering would be predicted because of the
loss of intermediate filament-binding proteins in the desmosome. The
head domain of PKP-1 but not the armadillo repeat domain binds to and
recruits desmoplakin to cell borders (Figs. 1 and 4), highlighting a
fundamental difference between PKP-1 and plakoglobin. In the case of
plakoglobin, desmoplakin binds directly to the central armadillo
motifs, and, although the first three repeats retain some binding
ability, the entire collection of 13 repeats is required for a robust
interaction (not shown). The fact that
the PKP-1 armadillo domain remained diffuse in the cytoplasm was
somewhat surprising because the arm repeats of plakoglobin,
Previous studies suggest that lateral interactions among desmosomal
components are critical to the assembly process (8, 10). Together with
the data presented here showing that PKP-1 enhances desmoplakin
recruitment to the plasma membrane, these observations are consistent
with the model in Fig. 5. In the absence of PKP-1, the number of available desmosomal cadherin-plakoglobin complexes would limit the total amount of desmoplakin present at the
junction. However, the presence of PKP-1 would overcome this limitation
by providing additional desmoplakin-binding sites at the membrane.
Consistent with this, increased desmosomal localization of endogenous
desmoplakin was observed in COS cells transiently expressing PKP-1 (not
shown). The model also predicts that PKP-1 could associate laterally
with multiple desmoplakin molecules, which might occur if PKP-1 forms
dimers or multimers or if each PKP-1 molecule has multiple
desmoplakin-binding sites. Because our present data cannot provide
quantitative information on the stoichiometry of PKP-1·DP complexes,
future work will be needed to test these possibilities. However, if
PKP-1 were to associate with at least two desmoplakin molecules, this
would provide an explanation for its ability to enhance DP-NTP
recruitment to cell borders in the absence of exogenously expressed
cadherins and plakoglobin. Secondary interactions between PKP-1 and the
desmosomal cadherins might also occur, leading to further strengthening
of the adhesive complex (see also Ref. 10).
The data presented in this study also suggest that plakoglobin and
PKP-1 exhibit fundamentally different modes of assembly into the
desmosomal plaque, with plakoglobin linking desmosomal cadherins to
desmoplakin and PKP-1 functioning largely in lateral interactions.
Consistent with this hypothesis is the observation that desmosomes in
suprabasal layers of the epidermis are larger than simple epithelial
desmosomes or desmosomes from basal cells. During epidermal
differentiation, desmosomes may increase in size and stability because
of insertion of PKP-1/DP-complexes, thereby enhancing desmosome
interactions with the cytoskeleton and rendering cells more resistant
to mechanical stress. Presumably, this architectural arrangement of
both linear and lateral interactions provides for a strong adhesive
junction with multiple protein-protein interactions as targets for
cellular regulation.
We thank Drs. M. Wheelock and K. Johnson for
providing antibody reagents, Dr. S. Elledge for providing yeast
two-hybrid reagents, and Dr. N. Clipstone for the use of the Fluoroscan
plate reader.
*
This work was supported by March of Dimes Grant FY98-0073,
and by National Institutes of Health Grants RO1AR43380 and PO1DE12328 (to K. J. G.) and K01 AR02039 (to A. P. K.), and by
DFG Grants Ha 1791/3-1, 3-2, and 3-3 (to M. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
§
Present address: Dept. of Dermatology, Emory University School of
Medicine, Woodruff Memorial Bldg., Rm. 5007, 1639 Pierce Dr., Atlanta,
GA 30322.
**
To whom correspondence should be addressed: Dept. of Pathology,
Northwestern University Medical School, 303 East Chicago Ave., Chicago,
IL 60611. Tel.: 312-503-5300; Fax: 312-503-8240; E-mail: kgreen{at}nwu.edu.
2
M. Hatzfeld, manuscript in preparation.
3
M. Hatzfeld, M. Ruediger, and E. Klaile,
unpublished observations.
4
M. Hatzfeld, unpublished observations.
The abbreviations used are:
PKP-1, plakophilin-1;
Ab, antibody;
mAb, monoclonal antibody;
CMV, cytomegalovirus;
PCR, polymerase chain reaction.
COMMUNICATION
The Head Domain of Plakophilin-1 Binds to Desmoplakin and
Enhances Its Recruitment to Desmosomes
IMPLICATIONS FOR CUTANEOUS DISEASE*
§,
,,,,, and**
Pathology and
Dermatology and the Robert H. Lurie Cancer Center,
Northwestern University Medical School, Chicago, Illinois 60611 and the
¶ Molecular Biology Group of the Medical Faculty,
Martin-Luther-University of Halle, Magdeburger Strasse 18, 06097 Halle/Saale, Germany
ABSTRACT
TOP
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS
DISCUSSION
REFERENCES
INTRODUCTION
TOP
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS
DISCUSSION
REFERENCES
-catenin (4). The
desmosomal cadherin-plakoglobin complex is coupled to the intermediate
filament network by desmoplakin (5, 6), which binds to both plakoglobin
and intermediate filaments (7-10).
EXPERIMENTAL PROCEDURES
TOP
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS
DISCUSSION
REFERENCES
Gly)
compared with the published sequence (GenBankTM accession
number X56654). To assay for interactions between proteins, yeast
(strain HF7c) were transformed with constructs of interest, and
-galactosidase activity was monitored using 4-methylumbelliferyl
-D-galactopyranoside as a substrate (9, 23).
Transformants were also tested for growth in the absence of histidine
using 25 mM 3-aminotriazole, and growth was monitored spectrophotometrically (A600) as an assay for
protein interactions.
RESULTS
TOP
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS
DISCUSSION
REFERENCES
View larger version (104K):
[in a new window]
Fig. 1.
PKP-1 enhances recruitment of the desmoplakin
amino-terminal domain to cell borders. COS cells were transiently
transfected (T) with DP-NTP alone (A and
B) or in the presence of PKP-1 (C and
D) or the PKP-1 head (E and F) or
armadillo repeat domain (Arm; G and
H). Cells in A-F were extracted in 0.01%
saponin prior to methanol fixation. PKP-1 or the PKP-1 head domain but
not the armadillo repeat domain localized and recruited DP-NTP to
cell-cell borders.
View larger version (58K):
[in a new window]
Fig. 2.
Dsg1 co-immunoprecipitates with plakoglobin
but not PKP-1. Dsg1 was transiently expressed in COS cells alone
or in the presence of either plakoglobin or PKP-1. In cells
co-expressing plakoglobin and Dsg1 (A), plakoglobin
antibodies co-immunoprecipitated (IP) Myc-tagged Dsg1. In
contrast, an antibody directed against the PKP-1 head
immunoprecipitated PKP-1 but not Dsg1 (B). Note that COS
cells express some endogenous plakoglobin. The asterisk in
B identifies PKP-1. The 51-kDa bands represent IgG.
View larger version (22K):
[in a new window]
Fig. 3.
PKP-1 forms complexes with the amino-terminal
domain of desmoplakin. DP-NTP was transiently expressed in COS
cells either alone or in the presence of PKP-1. M2 antibody-coupled
beads were used to immunoprecipitate FLAG-tagged DP-NTP and associated
proteins. Immunoblot analysis was carried out using antibodies directed
against PKP-1 or DP-NTP. PKP-1 co-immunoprecipitated (IP)
with DP-NTP (70 kDa) and was not precipitated by M2 antibody-agarose
beads in the absence of DP-NTP.
-galactosidase reporter
assay (Fig. 4). The PKP-1 head domain
also interacted with the Dsg1 cytoplasmic tail in this assay, but a
significant interaction with the Dsc2a cytoplasmic domain was not
detected. The PKP-1 armadillo repeat domain did not bind to either
DP-NTP or to the desmosomal cadherin cytoplasmic tail domains. This is in contrast to the armadillo repeat domain of plakoglobin, which does
bind to DP-NTP (8, 23). Similar results were obtained using growth in
the absence of histidine as the reporter for protein interactions (not
shown).
View larger version (30K):
[in a new window]
Fig. 4.
DP-NTP binds directly to the PKP-1 head
domain. Yeast two-hybrid analysis was used to define domains of
PKP-1 that interact with DP-NTP using a -galactosidase assay and the
substrate 4-methylumbelliferyl -D-galactopyranoside
(MUG) as a reporter assay for protein interactions. The
PKP-1 head domain and armadillo repeat domain (Arm) were
tested for interactions with DP-NTP, the cytoplasmic tail of
desmoglein-1 (Dsg1), or the cytoplasmic tail of
desmocollin-2a (Dsc2). Interactions between p53 and large T
antigen (LgT) are shown as a positive control. The head
domain of PKP-1 binds directly to the amino-terminal domain of DP-NTP.
As reported for full-length PKP-1 (10), the PKP-1 head domain also
interacts with Dsg1, although this interaction was not detected in
immunoprecipitates from cell lysates (Fig. 2). For this representative
experiment, each bar represents the average of quadruplicate
measurements for an independent clone.
DISCUSSION
TOP
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS
DISCUSSION
REFERENCES
-catenin, p120, and p00713 all bind to
cadherins (31). PKP-1 does bind to some desmosomal cadherins when
tested by in vitro overlay assays4
(10, 32), and PKP-1 did interact with Dsg1 in the yeast two-hybrid assay. However, the interaction was between Dsg1 and the non-armadillo head domain of PKP-1 (Fig. 4). Furthermore, in contrast to plakoglobin (8, 23), transfection experiments demonstrated that full-length PKP-1
does not require co-expression with a cadherin to localize and recruit
DP-NTP to cell-cell borders (Fig. 1). It is possible that PKP-1
preferentially associates with certain isoforms of desmosomal cadherins
that are co-expressed with PKP-1 during epidermal differentiation, such
as Dsg1 and or Dsc1. However, it appears that the primary binding
partner for PKP-1 is desmoplakin and that equimolar amounts of
cadherin·PKP-1 are not required for PKP-1 assembly into the plaque.
View larger version (25K):
[in a new window]
Fig. 5.
A model for desmosome assembly. In the
presence of PKP-1, there is an increase in desmoplakin (DP)
recruitment and enhanced intermediate filament attachment. In the
absence of PKP-1, the number of available cadherin-plakoglobin
(PG) complexes would limit desmoplakin accumulation at the
membrane. The schematic summarizes current information regarding the
hierarchy of interactions among desmosomal components; however, a
determination of the absolute stoichiometry of these interactions
awaits future study.
ACKNOWLEDGEMENTS
FOOTNOTES
ABBREVIATIONS
REFERENCES
TOP
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS
DISCUSSION
REFERENCES
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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 R. B. Presland and B. A. Dale Epithelial Structural Proteins of the Skin and Oral Cavity: Function in Health and Disease Critical Reviews in Oral Biology & Medicine, January 1, 2000; 11(4): 383 - 408. [Abstract] [Full Text] [PDF]
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A. North, W. Bardsley, J Hyam, E. Bornslaeger, H. Cordingley, B Trinnaman, M Hatzfeld, K. Green, A. Magee, and D. Garrod Molecular map of the desmosomal plaque J. Cell Sci., January 12, 1999; 112(23): 4325 - 4336. [Abstract] [PDF]
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C. A. Gaudry, H. L. Palka, R. L. Dusek, A. C. Huen, M. J. Khandekar, L. G. Hudson, and K. J. Green Tyrosine-phosphorylated Plakoglobin Is Associated with Desmogleins but Not Desmoplakin after Epidermal Growth Factor Receptor Activation J. Biol. Chem., June 29, 2001; 276(27): 24871 - 24880. [Abstract] [Full Text] [PDF]
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