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J Biol Chem, Vol. 274, Issue 26, 18153-18156, June 25, 1999
,From the Institut für Zellbiochemie und klinische Neurobiologie, Universität Hamburg, Martinistrasse 52, 20246 Hamburg, Germany
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ABSTRACT |
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 TOP
 ABSTRACT
 INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
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We report here an interaction between the C
terminus of the rat somatostatin receptor subtype 2 (SSTR2) and a
protein that has recently been identified as cortactin-binding protein
1 (CortBP1). Interaction is mediated by the PDZ (PSD-95/discs
large/ZO-1) domain of CortBP1. As shown by in situ
hybridization, SSTR2 and cortactin-binding protein are coexpressed in
the rat brain. The association between SSTR2 and the PDZ-domain of
CortBP1 was verified by overlay assays and by coprecipitation after
transfection in human embryonic kidney (HEK) cells. Analysis by
confocal microscopy indicates that CortBP1 is distributed diffusely
throughout the cytosol in transfected cells and that it becomes
concentrated at the plasma membrane when SSTR2 is present. This process
is largely increased when the receptor is stimulated by somatostatin;
as CortBP1 interacts with the C terminus of SSTR2, our data suggest
that the binding of agonist to the receptor increase the accessibility
of the receptor C terminus to the PDZ domain of CortBP1. Our data for
the first time establish a link between a G-protein coupled receptor
and constituents of the cytoskeleton.
Neuronal receptors for chemical transmitters are not uniformly
distributed throughout the cell but are concentrated at specific cellular sites; this is particularly true for receptors belonging to
the group of ligand-gated ion channels, which are clustered at
postsynaptic sites through interaction with specific proteins such as
rapsyn (1), gephyrin (2), or the PSD/SAP proteins (3). In contrast,
very little is known about proteins that are involved in the targeting
of G-protein-coupled receptors
(GPCR)1 to their sites of
action. Proteins that are known to interact intracellularly with this
group of receptors are either involved in the function (G-proteins) or
in the regulation (arrestins and the receptor kinases) of GPCRs (4),
but not in the subcellular localization. Only recently several reports
have suggested that additional proteins may interact with certain GPCRs
(5-8). However, for the large majority of GPCRs it remains unclear if
specific proteins exist that are responsible for anchoring or
subcellular targeting of the receptors.
We have addressed this issue by searching for proteins that
interact with the intracellular C terminus of receptors for the neuropeptide somatostatin (SST). Somatostatin acts through five different G-protein-coupled receptors (SSTR1-5), which are widely expressed in the mammalian central nervous system; frequently more than
one receptor subtype is detectable in one cell type (9), and it may be
difficult to assign the effects of somatostatin and its analogues to
any specific receptor subtype. One possible reason for this
multiplicity of subtypes may be the differential subcellular
localization that has recently been observed using subtype-specific
antibodies (10-13).
Here we show that the C terminus of the rat SSTR2 interacts
specifically with the PDZ domain of a cortactin-binding protein 1 (CortBP1). As the C-terminal sequences of SSTRs are largely divergent,
our data suggest that the specific targeting of receptor subtypes may
be achieved by protein interactions involving this part of the receptor molecule.
Yeast Two-hybrid Screen--
A cDNA fragment (nucleotide
residues 1318-1477) coding for the last 53 amino acids residues of the
C terminus of the rat SSTR2 (14) was cloned into the yeast bait vector
pAS-2 (CLONTECH). After transformation into the
yeast reporter strain CG-1945, a human brain cDNA library in the
bait vector pACTII (CLONTECH) was screened for
interacting proteins using protocols available from
CLONTECH and from the Gietz laboratory
(http://www.umanitoba.ca/faculties/medicine/units/human_genetics/gietz). Out of a total of 3-4 × 106 transformants, five
positives were obtained.
Generation of Fusion Proteins and Antisera--
cDNA
fragments coding for potentially interacting proteins were cloned into
the glutathione S-transferase fusion protein vector pGEX-2T
(Amersham Pharmacia Biotech, Freiburg, Germany); fusion proteins were
expressed in Escherichia coli strain XL1 Blue and purified
on glutathione-Sepharose (15).
The C terminus of the rat SSTR2 was cloned into the expression vector
ppXa-3 (Promega, Madison, WI), which leads to the expression of
biotinylated fusion proteins. These were also expressed in XL1 Blue
bacteria and purified using the PinPoint purification system (Promega)
according to the manufacturer's instructions. GST fusion proteins of
the PDZ domains of synapse-associated protein 102 (SAP102) were
obtained from Dr. Craig Garner (University of Alabama, Birmingham, AL).
A GST fusion protein containing the PDZ domain of clone 16 was used for
the immunization of rabbits; 100 µg of purified protein was used for
immunization in complete (first immunization only) or incomplete
Freund's adjuvant (Sigma, Munich, Germany). Serum obtained after the
third boost (189.3) was used for all experiments described here.
Overlay Assays--
GST fusion proteins were fractionated by
SDS-polyacrylamide gel electrophoresis and transferred onto a
nitrocellulose membrane (Protran; Schleicher & Schuell, Dassel,
Germany). Membranes were blocked and proteins renatured in TBS-T (50 mM Tris-HCl, pH 7.9, 150 mM NaCl, 0.05% Tween
20) supplemented with 3% bovine serum albumin for 12 h at
4 °C. The overlay was initiated by incubating the membranes in TBS-T
supplemented with 0.3% bovine serum albumin and 3 µg/ml biotinylated
fusion protein at room temperature for 4 h under constant shaking.
After washing the biotinylated probes were detected using alkaline
phosphatase-conjugated avidin.
In Situ Hybridization--
Whole brains of adult rats were
frozen on dry ice, and 20-µm sections were prepared on a cryostat
(Leitz, Wetzlar, Germany). Antisense RNA probes labeled with
Expression in HEK Cells and Coimmunoprecipitation--
The
cDNAs for SSTR2 carrying an N-terminal T7-epitope tag (17, 18) and
CortBP1 (donated by Dr. J. Thomas Parsons) were coexpressed in HEK
cells by transient transfection using the calcium phosphate method
(19). Cells were lyzed in radioimmune precipitation buffer (1% Nonidet
P-40, 0.5% sodium deoxycholate, 0.1% SDS, 150 mM NaCl, 50 mM Tris-HCl, pH 7.4), and the epitope-tagged receptor was
precipitated from the supernatant fraction using the monoclonal T7-antibody as described (18). Precipitates were analyzed by Western
blotting; CortBP1 was detected using the anti-PDZ domain antibody as a
primary antibody and goat-anti-rabbit IgG coupled to alkaline
phosphatase (Santa Cruz Biotechnology Inc., Santa Cruz, CA) as
secondary antibody. The efficiency of the precipitation was checked by
immunoblotting using an anti-SSTR2 polyclonal antiserum (antiserum
6291, donated by Dr. Stefan Schulz, Magdeburg, Germany) as primary antibody.
Confocal Microscopy--
For the colocalization of SSTR2 and
CortBP1, transfected HEK cells were plated on
poly-D-lysine-coated glass coverslips. After incubation in
normal growth medium for 3 days, cells were fixed using 4%
paraformaldehyde in phosphate-buffered saline (PBS) as described (17)
and permeabilized in 0.1% Triton X-100 in PBS for 90 s. After
incubation with a mixture of T7 monoclonal antibody and the 189.3 rabbit polyclonal antiserum (1:5,000 in PBS containing 2% normal goat
serum) overnight at 4 °C, cy2-conjugated goat-anti mouse and
cy3-conjugated goat-anti rabbit were used as secondary antibodies (18).
Cells were viewed with a confocal microscope (Leitz laser scanning
microscope) using specific settings for cy2 (argon laser/excitation at
488 nm/emission band pass 510-525 nm) and cy3 (helium-neon
laser/excitation at 543 nm/emission low pass 570 nm). The absence of
bleed-through between the two fluorophores was verified by performing
parallel staining experiments on cells expressing either one or the
other antigen only.
Identification of SSTR2-interacting Proteins--
The
intracellular C-terminal tail of the rat SSTR2 was used as bait in a
yeast two-hybrid screen of a human brain cDNA library. In this
screen five positive clones were obtained, which were identified as the
human isoform of synapse-associated protein 102 (SAP102, three
independent clones; Ref. 20), syntrophin
To analyze whether SSTR2 and CortBP1 are coexpressed in the same
regions of the rat brain, in situ hybridization experiments were carried out. A striking overlap between the expression pattern of
the mRNAs coding for SSTR2 and CortBP1 was observed. Prominent expression of both mRNAs was detected in the cortex, the CA1, CA2,
and CA3 regions of the hippocampus and in the medial habenula (Fig.
2). No labeling was observed in control
sections that had been hybridized with sense RNA probes (data not
shown).
CortBP1 Interacts with the SSTR2 when Expressed in HEK
Cells--
CortBP1 was coexpressed with an epitope-tagged version of
the rat SSTR2 in HEK cells (Fig. 3). The
T7-tag was introduced at the N terminus of the receptor in order to
avoid interference with the PDZ-binding motif at the receptor C
terminus. When the receptor was precipitated from cellular extracts
using an anti-T7 monoclonal antibody, Western blotting analysis could
readily detect CortBP1 in the precipitate. In a control experiment, the
180-kDa band specific for CortBP1 was not observed when cells were
transfected with CortBP1 only (Fig. 3).
The cellular location of CortBP1 was examined in HEK cells transiently
transfected with either CortBP1 alone or with SSTR2 and CortBP1 (Fig.
4). In the absence of SSTR2 CortBP1
exhibits an exclusively cytoplasmic staining pattern. The nucleus is
spared, and there is no concentration of CortBP1 at the plasma
membrane. When cDNA coding for SSTR2 is added to the transfection
mixture, fluorescence label specific for the receptor is detectable at the cell surface, and only limited intracellular staining can be
observed. In these cells, the subcellular localization of CortBP1 undergoes a significant change, as it becomes concentrated at the cell
surface. This effect is somewhat variable, as illustrated by the two
examples in Fig. 4; in some cells there is still substantial intracellular staining for CortBP1 and only a moderate increase of
surface staining. In others, almost exclusive staining at the surface
can be observed. This may depend on the relative expression levels of
both proteins in individual cells. However, surface staining for
CortBP1 becomes much more prominent in cells that were treated with
somatostatin for 5 min. Under these conditions some receptors already
start to migrate into intracellular vesicles due to
agonist-dependent endocytosis (18), whereas the majority of
the receptor-specific fluorescence is still located on the cell
surface. In all cells examined that did coexpress SSTR2 and CortBP1,
CortBP1 exhibited strong plasma membrane staining when the receptor had
been stimulated with agonist. These data suggest that the C terminus of
the rat SSTR2 is involved in the structural rearrangements induced by
the agonist.
In this report we have identified a protein that interacts
specifically with the C terminus of one of the five somatostatin receptor subtypes, SSTR2. CortBP1 is abundantly expressed in the mammalian central nervous system in a pattern showing strong overlap with the expression pattern of SSTR2, suggesting that the interaction observed is likely to occur in a wide variety of neuronal cell types.
Interaction between SSTR2 and its binding protein is likely to be
directed by the receptor C terminus, as the C-terminal sequence of
SSTR2 (Q-T-S-I-Stop) contains the consensus sequence for recognition of
PDZ domains, i.e. (S/T)-X-(V/I)-Stop, where
X can be any amino acid residue (3, 23). Indeed the
interaction between the SSTR2 bait and its target obtained in the yeast
screen is abolished when the C terminus is mutated (data not shown).
CortBP1 is a multidomain protein that contains multiple
SH3-binding sites and a SAM domain; CortBP1 interacts with the
cytoskeletal protein cortactin via the SH3-domain of cortactin and is
thus linked to cortical actin filaments (22). Therefore we propose that
the interaction of SSTR2 with CortBP1 provides a physical link between
a G-protein-coupled receptor and the cytoskeleton, which could be
important for immobilizing the SSTR2 at specific sites in the membrane.
It is noteworthy that CortBP1 (and cortactin) was prominently detected
in the axonal growth cones of hippocampal neurons in culture (22). Thus
CortBP1 could be responsible for anchoring SSTR2 in nerve terminals,
where it has been localized by immunocytochemistry in rat brain and
where it functions as a presynaptic receptor in the regulation of
transmitter release via the inhibition of N-type calcium channels (10,
24).
In transfected cells, CortBP1 undergoes a dramatic relocalization to
the plasma membrane if SSTR2 is cotransfected. This effect is enhanced
when the receptor is stimulated with agonists, suggesting that an
increased proportion of the receptor becomes accessible at its C
terminus. A similar effect has been observed before (6) demonstrating
that the C terminus of the
INTRODUCTION
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
MATERIALS AND METHODS
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
-35S-UTP (NEN Life Science Products) were generated
using the rat SSTR2 cDNA (14) and a rat cortactin-binding protein
clone obtained from Dr. J. T. Parsons (University of Virginia,
Charlottesville, VA). In situ hybridization experiments were
performed as described (16). Sections were exposed to BioMax MR film
for 3 days.
RESULTS
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
1 (21) and a novel protein
fragment (clone 16), which contains a PDZ domain that is highly
homologous (89% identity) to the PDZ domain of the rat
cortactin-binding protein 1 (CortBP1; Ref. 22; see Fig.
1A). As SAP102 and syntrophin
1 also contain PDZ domains, these results indicated a preference of
the SSTR2 C terminus for interactions with PDZ domains. To identify
which of these proteins might indeed interact with the somatostatin
receptor subtype 2, GST fusion proteins of the PDZ domains of SAP102,
syntrophin and CortBP1, were expressed and purified in E. coli. Binding to the SSTR2 C terminus was analyzed in an overlay
assay using a biotinylated SSTR2 fusion protein as a probe (20). In
this assay, the full-length PDZ domain of CortBP1 and some smaller
proteolytic fragments thereof elicited a strong response (Fig.
1B). The strong reaction by the smaller fragments (which
appear to be only minor contaminants when judged from the Coomassie
stained gel) may reflect a better ability of these fragments to refold
after SDS-gel electrophoresis. In contrast to CortBP1, the PDZ domains
of SAP102 and syntrophin showed no reaction (Fig. 1B). No
response was also observed when the overlay reaction was performed with
a biotinylated control protein derived from the empty pinpoint Xa3
vector (data not shown). These results suggest that the interaction
between the C terminus of SSTR2 and the PDZ domain of the CortBP1 is of
high affinity, whereas the interaction with the other proteins
containing PDZ domains is of low affinity, the latter of which were
obviously sufficient to obtain a positive signal in the yeast
two-hybrid screen but are not likely to be of physiological
significance.
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Fig. 1.
Interaction of CortBP1 with the SSTR2 C
terminus. A, sequence alignment of the human PDZ-domain
protein fragment and CortBP1. Shown is a sequence alignment between the
PDZ domains of the human fragment (clone 16) obtained by the yeast
two-hybrid screen and CortBP1. Identical amino acids are denoted by
vertical bars and similar amino acids by dots.
B, overlay assay. GST fusion proteins of the PDZ domains of
proteins detected by the yeast two-hybrid screen were run on
SDS-polyacrylamide gels and either stained with Coomassie Brilliant
Blue (left panel) or blotted onto nitrocellulose membranes
and probed with the biotinylated fusion protein containing the SSTR2 C
terminus (right panel). Specifically bound fusion protein
was detected using alkaline phosphatase coupled to avidin. SAP102 R123
contains all three domains, but SAP102 R1 only the first PDZ
domain.
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Fig. 2.
Comparison of the expression patterns of
SSTR2 and CortBP1 in the rat brain. Adjacent coronal sections from
frozen adult rat brains were probed with 35S-labeled
antisense cRNA of rat SSTR2 (A) or rat CortBP1
(B). Cx, cortex; Hi, hippocampus;
MHb, medial habenula.
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Fig. 3.
Association of SSTR2 with CortBP1 in
transfected HEK cells. HEK cells were transiently transfected with
expression vectors for rat CortBP1 either alone or in combination with
Ntag-SSTR2. The first two lanes show Western blots from cellular
lysates using the 189.3 antiserum which recognizes CortBP1. The
two right lanes show Western blots of immunoprecipitates
(IP) where the SSTR2 was precipitated from cellular lysates
using the T7 antibody directed against the epitope tag at the N
terminus of the receptor. Note the absence of staining in lanes where
SSTR2 cDNA was omitted from the transfection mixture.
View larger version (61K):
[in a new window]
Fig. 4.
Colocalization in HEK cells. Cells
expressing either CortBP1 (A) or CortBP1 and SSTR2
(B) were stained with antibodies directed against CortBP1
and the T7-tag at the N terminus of SSTR2. Cells were examined by
confocal microscopy, and optical sections were obtained from the center
of the cells. In A only the CortBP1-specific fluorescence is
shown, whereas in B fluorescence signals were recorded from
the cy2/SSTR2-specific channel (upper panels) and the
cy3/CortBP1 specific channel (lower panels).
Arrows indicate the positions where fluorescence specific
for CortBP1 is enriched at the plasma membrane; arrowheads
point at the position of endocytotic vesicles containing SSTR2.
DISCUSSION
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
-adrenergic receptor interacts with a PDZ
domain of the regulatory factor of the Na+/H+
exchanger only if the receptor is stimulated by agonists. This interaction leads to transduction of a signal from the receptor to the
exchanger protein (6). On a structural level, these and our data imply
that the C-terminal intracellular tail of G-protein-coupled receptors
is somehow involved in the structural rearrangements that take place
after activation.
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ACKNOWLEDGEMENTS |
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We thank Hans-Hinrich Hönck for excellent technical assistance, Tilmann Breiderhoff for preparing the SSTR2-ppXa-3 construct, Chica Schaller and Irm Hermans-Borgmeyer (Zentrum für Molekulare Neurobiologie, Hamburg, Germany) for help with the in situ hybridization experiments, J. Thomas Parsons (University of Virginia, Charlottesville, VA) for providing the CortBP1 clone, Craig Garner (University of Alabama, Birmingham, AL) for SAP102 fusion proteins, and Stefan Schulz (University of Magdeburg, Magdeburg, Germany) for SSTR2 antibodies.
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FOOTNOTES |
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* This work was supported by the Deutsche Forschungsgemeinschaft (SFB545/B7 (to H.-J. K. and D. R.)).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.
The data presented here form part of a thesis by H. Z.
§ To whom correspondence should be addressed: Institut für Zellbiochemie und klinische Neurobiologie, Universität Hamburg, Martinistrasse 52, 20246 Hamburg, Germany. Tel.: 49-40-42803-3344; Fax: 49-40-42803-4541; E-mail: richter{at}uke.uni-hamburg.de.
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ABBREVIATIONS |
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The abbreviations used are: GPCR, G-protein-coupled receptor; CortBP1, cortactin-binding protein 1; GST, glutathione S-transferase; HEK, human embryonic kidney; PBS, phosphate-buffered saline; PDZ, PSD-95/discs large/ZO-1; PSD, postsynaptic density; SAP102, synapse-associated protein 102; SST, somatostatin; SSTR, somatostatin receptor.
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REFERENCES |
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TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
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