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Volume 272, Number 47, Issue of November 21, 1997
pp. 29407-29410
(Received for publication, September 3, 1997, and in revised form, September 24, 1997)
From the ABSTRACT We have cloned a cDNA encoding a novel
protein of 302 amino acids (designated Noc2, no C2 domain)
that has 40.7% amino acid identity with and 77.9% similarity to the
N-terminal region of rabphilin-3A, a target molecule of Rab3A. However,
unlike rabphilin-3A, Noc2 lacks two C2 domains that are thought to
interact with Ca2+ and phospholipids. Noc2 is
expressed predominantly in endocrine tissues and hormone-secreting cell
lines and at very low levels in brain. Immunoblot analysis of
subcellular fractions of the insulin-secreting cell line MIN6 and
immunocytochemistry reveal that Noc2 is a 38-kDa protein present in the
cytoplasm. Overexpression of Noc2 in PC12 cells cotransfected with
growth hormone enhances high K+-induced growth hormone
secretion. Screening a mouse embryonic cDNA library with the yeast
two-hybrid system shows that Noc2 interacts with the LIM
domain-containing protein zyxin, a component of the cytoskeleton, and
this interaction is further confirmed by the coimmunoprecipitation
experiment. Accordingly, Noc2 is probably involved in regulated
exocytosis in endocrine cells by interacting with the cytoskeleton.
INTRODUCTION Exocytosis is a key step in neurotransmitter and hormone
secretions from neurons and endocrine cells, respectively (1, 2). These
secretions are regulated by Ca2+, which triggers exocytosis
(3). In neurons, the small GTP-binding protein Rab3A plays an important
role in exocytosis of synaptic vesicles (4, 5). Rabphilin-3A, a
putative target of Rab3A (6), has been suggested to be involved in the
recruitment of synaptic vesicles for exocytosis by Rab3A (7, 8).
Although, like synaptotagmins, which are a candidate for calcium sensor in neurotransmitter release (9), rabphilin-3A has two repeats of the C2
domain (regulatory domain of protein kinase C that confers Ca2+ and phospholipid binding) in the C-terminal half,
rabphilin-3A is unique in that it has a Rab3A-binding domain in the
N-terminal region (6). The recently identified Doc2 EXPERIMENTAL PROCEDURES 700,000 plaques of a rat islet
cDNA library were hybridized under low stringency conditions (17)
using a mouse rabphilin-3A cDNA (16) as a probe. Five clones
encoded a partial rabphilin-3A-related protein (designated Noc2). A
full-length Noc2 clone was isolated from a RINm5F cDNA library.
Both strands of DNA were sequenced.
RNA blot analysis was performed under
standard stringent hybridization conditions with
32P-labeled 580-base pair Noc2 cDNA. Membranes were
washed with 0.1 × SSC, 0.1% SDS at 50 °C for 1 h and
were exposed to x-ray film with intensifying screen at Anti-Noc2 antiserum was raised by
immunizing rabbits with 17-mer peptide (GATDPQGGTLPRPEPRV)
corresponding to amino acid residues 274-290 of Noc2. The antisera
were purified through a protein G-Sepharose column (Pharmacia Biotech
Inc.). The anti-Noc2 and anti-synaptotagmin III antibodies (15) were
used in 1:1000 and 1:5000 dilution, respectively. Blots were probed
with these antibodies and horseradish peroxidase-conjugated secondary
antibodies (Amersham Corp.), and proteins were detected with ECL
reagent (Amersham Corp.).
Discontinuous sucrose gradient
fractionation of the insulin-secreting cell line MIN6 was performed
according to the method described by Wendland and Scheller (18) with
slight modifications (15). Each postnuclear fraction containing 2-20
µg of protein was precipitated with 15% of trichloroacetate,
separated on 10% SDS-polyacrylamide gel, and subjected to immunoblot
analysis.
MIN6 cells
grown on chamber slides were incubated in HEPES balanced Krebs-Ringer
buffer, fixed with 4% of paraformaldehyde, and permeabilized with
0.1% Triton X-100. Immunoreactivity of Noc2 was detected with
anti-Noc2 antibody and rhodamine-conjugated goat anti-rabbit IgG
(Jackson Immunoresearch Laboratories, West Grove, PA). Immunoreactivity
of insulin was detected with mouse monoclonal anti-rat insulin antibody
(Advanced Immuno Chemical, Long Beach, CA) and fluorescein
isothiocyanate-conjugated goat anti-mouse IgG (Jackson Immunoresearch
Laboratories) (15).
A
full-length cDNA of Noc2 or Yeast strain L40 (MATa trp1 leu2 his3
LYS2::lexA-HIS3 URA3::lexA-lacZ) was
transformed with a derivative of pBTM116 bearing a full-length Noc2
fused to the LexA DNA-binding domain (pBTM116-Noc2) using the lithium
acetate method (20). Strain L40 carrying pBTM116-Noc2 was transformed
with a mouse embryonic cDNA library. Approximately 1.96 × 106 transformants were screened for growth on Yc plate
medium (2% glucose, 0.5% ammonium sulfate, 1% succinic acid, and
0.12% yeast nitrogen base) containing 0.5 mM
3-amino-1,2,4-triazole but lacking tryptophan, histidine, uracil, and
leucine. His+ colonies were then placed on the paper
filters and stained with 5-bromo-4-chloro-3-indolyl- The protein coding region Noc2 cDNA
was subcloned in frame into pGEX-2T (Pharmacia). The pGEX-2T-Noc2 was
transformed into JM109. The expressed protein was affinity-purified by
glutathione-Sepharose 4B (Pharmacia). The N-terminal fragment of mouse
zyxin (amino acids 343-564) cDNA was subcloned in frame into
pFLAG-MAC (Kodak/IBI, New Haven, CT). The expressed protein was
affinity-purified by Anti-FLAG M2 Affinity Gel (Kodak/IBI), according
to the manufacturer's instructions. For coimmnoprecipitation
experiments, the purified GST-Noc2 (1 µg) was incubated at 4 °C
for 1 h with the purified FLAG-zyxin (1 µg) in the binding
buffer (50 mM Tris-HCl, pH 7.5, 5 mM
MgCl2, 100 mM NaCl, 10% glycerol, 0.5 mg/ml
bovine serum albumin, and 5 mM RESULTS The sequence of the longest insert (1934 base pairs) of
[View Larger Version of this Image (41K GIF file)]
RNA blot analysis revealed that a
single 2.2- or 2.6-kb transcript of Noc2 is expressed at very high
levels in pancreatic islets; at moderate to high levels in ovary,
adrenal, pituitary, and PC12 cells and the insulin secreting cell lines
RINm5F (rat), MIN6 (mouse), and HIT-T15 (hamster); and at low levels in
testis, the rat GH-secreting cell line GH3, and the mouse
adrenocorticotropic hormone-secreting cell line AtT20 (Fig.
2). Noc2 mRNA is detected at only
very low levels in brain after a longer exposure (data not shown). Noc2
protein is detected as a 38-kDa protein in total proteins prepared from
MIN6 cells and PC12 cells (data not shown).
[View Larger Version of this Image (35K GIF file)]
Fig.
3A shows the immunoblot
analysis of subcellular fractions prepared from MIN6 cells probed with
anti-Noc2 and anti-synaptotagmin III antibodies. Noc2 was detected as a
38-kDa protein in fractions 2-8, peaking at fraction 3. In contrast,
synaptotagmin III, which is present in large dense core vesicle in MIN6
cells (15), was detected in fraction at 9 and 10 (Fig. 3A).
Fig. 3B shows the representative of double-immunostaining of
MIN6 cell for Noc2 and insulin. Noc2 was detected diffusely and
partially dotted in the cytoplasm of MIN6 cells.
[View Larger Version of this Image (66K GIF file)]
Total amounts of GH produced in PC12 cells transfected with
human GH ranged from 3 to 10 ng/35-mm dish. The basal secretion of GH
(expressed as a percentage of GH amounts released into the medium
containing 4.7 mM K+ relative to amounts of
total cellular GH) is not significantly different between
Noc2-transfected (8.5 ± 0.87%) and control cells (8.7 ± 0.99%). Upon high K+ (60 mM) stimulation, GH
secretion from PC12 cells cotransfected with GH and Noc2 was
significantly higher than that seen in controls (Fig.
4).
[View Larger Version of this Image (16K GIF file)]
A putative target of Noc2 was
isolated from a mouse embryonic cDNA library by the yeast
two-hybrid system with the full-length Noc2 used as a bait. We isolated
four clones, one encoding a partial amino acid sequence of zyxin (amino
acids 353-509). FLAG-zyxin was specifically coimmunoprecipitated by
glutathione-Sepharose 4B (Fig. 5). In
addition, GST-Noc2 was also coimmunoprecipitated with zyxin by
Anti-FLAG M2 Affinity Gel (Fig. 5).
[View Larger Version of this Image (19K GIF file)]
DISCUSSION In the present study we have identified a novel protein designated
Noc2. Noc2 has structural features characterized by 1) a high degree of
similarity to the N-terminal region of rabphilin-3A, 2) no C2 domain,
and 3) no putative transmembrane region. Interestingly, Noc2 has a
putative zinc finger motif composed of a cysteine-rich sequence that is
conserved among rabphilin-3A and a recently identified putative Rab3
effector, RIM (21). Because rabphilin-3A has been shown to bind Rab3A
via this domain in a zinc-dependent manner (22), we assumed
that Noc2 might also interact with Rab3 members. However, Noc2 did not
bind Rab3A, Rab3B, or Rab3C under the conditions in which rabphilin-3A
binds Rab3A,2 although we
cannot exclude the possibility that Noc2 might bind other members of
the Rab3 subfamily or their related proteins.
To search for a molecule that interacts with Noc2, we screened a mouse
embryonic cDNA library using the yeast two-hybrid system (20) and
identified zyxin as a candidate. Coimmunoprecipitation experiments
confirmed that Noc2 interacts with zyxin. Zyxin is a cytoskeletal
element that exhibits an unusual proline-rich N terminus followed by
three tandemly arrayed LIM domains (23). The LIM domain contains the
cysteine-rich consensus sequence
CX2CX16-23HX2CX4CX2CX16-21CX2-3(C/H/D) (24). This domain participates in protein-protein interaction in a
zinc-dependent manner (24). It is possible, therefore, that
the zinc finger domain of Noc2 interacts with one of the LIM domains in
zyxin. In fact, we have found by the yeast two-hybrid system that the
zinc finger containing N-terminal fragment (amino acids 1-200) of Noc2
interacts with the fragment between the first and a part of the third
LIM domain of zyxin (data not shown).
Rabphilin-3A has been shown to interact with Although rabphilin-3A is expressed predominantly in brain, Noc2 is
expressed predominantly in endocrine cells and is poorly expressed in
brain. Overexpression of rabphilin-3A in PC12 cells enhances high
K+-induced GH secretion from the cells transfected with GH
(27). We have found that overexpression of Noc2 in PC12 cells also
enhances high K+-induced secretion, further suggesting
involvement of Noc2 in Ca2+-triggered secretion. Because
Noc2 lacks the C2 domain and is not present in large dense core vesicle
in MIN6 cells, it remains to be determined whether Noc2 interacts
directly or indirectly with vesicle-associated proteins having the C2
domain. Considering these findings together, Noc2 participates in
regulated exocytosis in endocrine cells probably by interacting with
the cytoskeleton.
FOOTNOTES The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF022774. ACKNOWLEDGEMENTS We thank S. Hollenberg for providing us with
the mouse embryonic cDNA library and A. Tamamoto for excellent
technical assistance.
REFERENCES
COMMUNICATION:
Noc2, a Putative Zinc Finger Protein Involved in Exocytosis in
Endocrine Cells*
,, and
Division of Molecular Medicine,
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS
DISCUSSION
FOOTNOTES
ACKNOWLEDGEMENTS
REFERENCES
and Doc2
also
have two repeats of the C2 domain, but lack the Rab3A-binding domain (10, 11). It has been shown that both rabphilin-3A and Doc2 also
influence regulated exocytosis in neurons (12, 13). Previously, we
identified synaptotagmin III, which is expressed at high levels in
endocrine tissues (14), and suggested that synaptotagmin III is a
candidate for the Ca2+ sensor in insulin release from
pancreatic -cells (15). However, the molecular basis of the
exocytosis-associated proteins in endocrine cells is not well known.
Although Rab3A is expressed in neuronal cells and endocrine cells,
rabphilin-3A is expressed exclusively in neurons and neuron-like cells
and is absent or present at very low levels in endocrine cells (16).
Reasoning that a putative target for Rab3A might be expressed
specifically in endocrine cells, we screened a rat pancreatic islet and
the insulin-secreting cell line RINm5F cDNA libraries using a DNA
fragment encoding the Rab3A-binding domain of rabphilin-3A as a probe.
We identified a novel protein that has a high similarity to the
Rab3A-binding domain of rabphilin-3A but lacks the C2 domain. Our data
also suggest that Noc2 is involved in regulated exocytosis in endocrine cells by interacting with the cytoskeleton.
80 °C for
36 h.
-galactosidase was inserted into the
mammalian expression vector pSR. PC12 cells, a rat
catecholamine-secreting cell line, were plated at a density of 3 × 105/35-mm dish and cultured in RPMI 1640 medium (Life
Technologies, Inc.) supplemented with 10% fetal bovine serum and 5%
horse serum. The cells were cotransfected with
GH1 expression vector pXGH5
(Nichols Institute, San Juan Capistrano, CA) (1 µg) and pSRNoc2 (1 µg) using LipofectAMINE (Life Technologies, Inc.), according to the
manufacturer's instructions. As controls, cells were cotransfected
with pXGH5 (1 µg) and pSRgal (1 µg). 3 days after
transfection, PC12 cells were washed with a PSS (140 mM
NaCl, 4.7 mM KCl, 2.5 mM CaCl2, 1.2 mM MgCl2, 1.2 mM
KH2PO4, 20 mM HEPES, pH 7.4, and 11 mM glucose) and incubated for 2.5, 5, or 10 min with a high
K+ solution (PSS containing 60 mM KCl and 85 mM NaCl) or a low K+ solution (PSS containing
4.7 mM KCl and 140 mM NaCl). GH was measured by
enzyme immunoassay kit (Picoia, Sumitomo, Osaka, Japan). Secretion was
expressed as a percentage of the GH amounts released into the medium
relative to the total cellular GH amounts (19).
-D-galactopyranoside for
-galactosidase activity as described (20). Four HIS+ and
LacZ+ positive clones were obtained with this screening.
The plasmids were recovered through Escherichia coli
transformation.
-mercaptoethanol), and
glutathione-Sepharose 4B (Pharmacia) was then added. The mixture was
incubated at 4 °C for 1 h. After washing three times with the
binding buffer, the mixture was eluted with the elution buffer (50 mM Tris-HCl, pH 7.5, 5 mM MgCl2,
100 mM NaCl, 10% glycerol, 5 mM
-mercaptoethanol, and 10 mM glutathione) and was then
subjected to immunoblot analysis. Coimmunoprecipitation with Anti-FLAG
M2 Affinity Gel (Kodak/IBI) was performed similarly.
clones contains an open reading frame encoding a
302-amino acid protein (Mr = 33431.2) having
40.7% identity with and 77.9% similarity to the amino acid sequence
of the N-terminal region (amino acids 1-304) of rat rabphilin-3A (Fig.
1). However, unlike rabphilin-3A, it
lacks the C2 domains and was therefore designated Noc2 (no
C2 domain). Interestingly, Noc2 has a putative metal ion-binding domain containing a cluster of cysteine residues that is also conserved
in rabphilin-3A. There are a potential protein kinase A-dependent phosphorylation site and three potential
protein kinase C-dependent phosphorylation sites in
Noc2.
Fig. 1.
Comparison of amino acid sequences of rat
Noc2 and rat rabphilin-3A. Amino acids are indicated in
single-letter codes. Identical and chemically similar amino acid
residues are indicated by double dots and single
dots, respectively. The N-terminal region (amino acid residues
1-304) of rat rabphilin-3A (Rabp) is shown. Potential
protein kinase A-dependent phosphorylation site and protein
kinase C-dependent phosphorylation sites of Noc2 are
indicated by * and #, respectively. Cysteine residues that constitute a putative zinc finger domain are boxed.
Fig. 2.
Northern blot analysis of Noc2. The
sizes of the hybridized transcripts of Noc2 are indicated. The size of
the transcripts of Noc2 is 2.2 kb in rat tissues and rat-derived
endocrine cell lines and 2.6 kb in mouse-derived cell lines. 20 µg of
total RNA, except for thyroid and pituitary (10 µg), were
loaded.
Fig. 3.
Subcellular localization of Noc2.
A, immunoblot analysis of postnuclear fractions. Upper
panel, Noc2; lower panel, synaptotagmin III
(Syt.III). Noc2 is detected as 38 kDa in fractions 2-8, and
synaptotagmin III is detected as 63 kDa in fractions 9 and 10. B, identification of Noc2 protein in MIN6 cells by confocal laser microscopy. MIN6 cells were immunostained with anti-Noc2 and
anti-insulin antibodies and visualized by fluorescence confocal microscopy. Left panel, Noc2; right panel,
insulin.
Fig. 4.
Effect of Noc2 overexpression on GH secretion
from PC12 cells. 
, effect of Noc2 on high K+ (60 mM)-induced GH secretion; 
, effect of Noc2 in basal GH
secretion; 
, control in high K+-induced GH secretion;
, control in basal GH secretion. Each point was assayed in duplicate
or triplicate. The values are the average of three independent
experiments. Filled squares and filled circles
are offset 1 min for clarity.
Fig. 5.
Coimmunoprecipitation of Noc2 and zyxin.
Lanes 1 and 4, GST-Noc2 alone (50 ng). Lane
2, FLAG-zyxin coimmunoprecipitated with GST-Noc2 by
glutathione-Sepharose 4B. Lanes 3 and 6,
FLAG-zyxin alone (30 ng). Lane 5, GST-Noc2
coimmunoprecipitated with FLAG-zyxin by Anti-FLAG Affinity Gel.
Upper panel, immunoblot analysis with anti-Noc2 antibody;
lower panel, immunoblot analysis with anti-FLAG M2
antibody.
-actinin, a component
of the cytoskeleton, and possibly to be involved in the predocking and
docking process of synaptic vesicles by linking Rab3A to the
cytoskeleton (25). This Rab3A-rabphilin-3A system is suggested to
regulate reorganization of actin filaments (25). Interestingly, a
proline-rich domain in the N-terminal region of zyxin has been shown to
interact with -actinin (26). Accordingly, Noc2 may participate in
the reorganization of actin filaments by interacting with zyxin.
To whom correspondence should be addressed. Tel.:
81-43-226-2187; Fax: 81-43-221-7803; E-mail:
seino{at}med.m.chiba-u.ac.jp.
1
The abbreviations used are: GH, growth hormone;
PSS, physiological salt solution; GST, glutathione
S-transferase; kb, kilobase(s).
2
T. Sasaki and Y. Takai, unpublished
observation.
Volume 272, Number 47,
Issue of November 21, 1997
pp. 29407-29410
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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