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A novel role of CPEB3 in regulating EGFR gene transcription via association with Stat5b in neurons

Peng, Shu-Chun, Lai, Yen-Ting, Huang, Hsi-Yuan, Huang, Hsien-Da, Huang, Yi-Shuian·2010·Nucleic Acids Research
DOI 10.1093/nar/gkq634PMC PMC2995057
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Figure 1. CPEB3 interacts with Stat5b. (A) Salient features of Stat5b showing the N-terminal region, coiled-coil domain, DNA-binding domain (DBD), Src-homology (SH2) and transactivation domain (TAD). The transcriptional activity of Stat5b is enhanced when the denoted tyrosine 699 (Y699) is phosphorylated upon growth hormone stimulation. When asparagine 642 mutated to histidine (N642H), it improves Stat5b’s activity by hindering dephosphorylation of phosphorylated Y699. Using the N-terminus (amino acids 1–427) of CPEB3 as the bait, a yeast two hybrid (Y2H) screen identified two clones corresponding to the amino acids 589–743 and 611–786 of Stat5b. The wild-type and truncated Stat5b mutants were tested for positive (+) or negative (–) interaction with the N-terminus of CPEB3. (B) Co-immunoprecipitation (Co-IP) assay. The plasmid expressing flag-Stat5b or a control EGFP along with plasmids encoding myc-tagged full-length (myc-CPEB3) and the C-terminal RNA-binding domain of CPEB3 (myc-CPEB3C) were cotransfected into 293T cells. The cell lysates were precipitated with flag antibody (Ab) and immunoblotted with myc Ab. IB: immunoblotting, IP: immunoprecipitation. (C) Reciprocal immunoprecipitation assay. The lysate from cortical neurons was precipitated with control, Stat5b or CPEB3 Ab and immunoblotted with CPEB3 and Stat5b Abs.
Figure 1. CPEB3 interacts with Stat5b. (A) Salient features of Stat5b showing the N-terminal region, coiled-coil domain, DNA-binding domain (DBD), Src-homology (SH2) and transactivation domain (TAD). The transcriptional activity of Stat5b is enhanced when the denoted tyrosine 699 (Y699) is phosphorylated upon growth hormone stimulation. When asparagine 642 mutated to histidine (N642H), it improves Stat5b’s activity by hindering dephosphorylation of phosphorylated Y699. Using the N-terminus (amino acids 1–427) of CPEB3 as the bait, a yeast two hybrid (Y2H) screen identified two clones corresponding to the amino acids 589–743 and 611–786 of Stat5b. The wild-type and truncated Stat5b mutants were tested for positive (+) or negative (–) interaction with the N-terminus of CPEB3. (B) Co-immunoprecipitation (Co-IP) assay. The plasmid expressing flag-Stat5b or a control EGFP along with plasmids encoding myc-tagged full-length (myc-CPEB3) and the C-terminal RNA-binding domain of CPEB3 (myc-CPEB3C) were cotransfected into 293T cells. The cell lysates were precipitated with flag antibody (Ab) and immunoblotted with myc Ab. IB: immunoblotting, IP: immunoprecipitation. (C) Reciprocal immunoprecipitation assay. The lysate from cortical neurons was precipitated with control, Stat5b or CPEB3 Ab and immunoblotted with CPEB3 and Stat5b Abs.CC BY-NC · PubMed Central
Figure 2. CPEB3 inhibits Stat5b-dependent transcription. (A) The 293T cells were transfected with plasmids encoding (i) EGFP, myc-CPEB3, myc-CPEB3 fused with the nuclear localization sequence (myc-CPEB3NLS) or myc-CPEB3C, and (ii) wild-type (WT) or constitutively active (CA) Stat5b with N642H mutation, and (iii) reporters expressing firefly luciferase driven by the IGF1 promoter containing two wild-type or mutated Stat5b-binding sites along with Renilla luciferase. TK: thymidine kinase promoter. Stat5b-mediated transactivation is expressed as fold of induction of normalized luciferase activity (firefly/Renilla) obtained in the presence of CA verse WT Stat5b. Three independent experiments were analyzed and expressed as mean ± s.e.m. and the asterisks denote significant difference (Student’s t-test). (B) Subcellular distribution of myc-CPEB3, myc-CPEB3NLS and myc-CPEB3C in 293T cells. (C) CPEB3 interacts similarly with Stat5b and Stat5bCA. The extracts containing myc-CPEB3 and WT or CA flag-Stat5b, were precipitated with myc Ab and probed with flag, p-Stat5b and myc Abs.
Figure 2. CPEB3 inhibits Stat5b-dependent transcription. (A) The 293T cells were transfected with plasmids encoding (i) EGFP, myc-CPEB3, myc-CPEB3 fused with the nuclear localization sequence (myc-CPEB3NLS) or myc-CPEB3C, and (ii) wild-type (WT) or constitutively active (CA) Stat5b with N642H mutation, and (iii) reporters expressing firefly luciferase driven by the IGF1 promoter containing two wild-type or mutated Stat5b-binding sites along with Renilla luciferase. TK: thymidine kinase promoter. Stat5b-mediated transactivation is expressed as fold of induction of normalized luciferase activity (firefly/Renilla) obtained in the presence of CA verse WT Stat5b. Three independent experiments were analyzed and expressed as mean ± s.e.m. and the asterisks denote significant difference (Student’s t-test). (B) Subcellular distribution of myc-CPEB3, myc-CPEB3NLS and myc-CPEB3C in 293T cells. (C) CPEB3 interacts similarly with Stat5b and Stat5bCA. The extracts containing myc-CPEB3 and WT or CA flag-Stat5b, were precipitated with myc Ab and probed with flag, p-Stat5b and myc Abs.CC BY-NC · PubMed Central
Figure 3. CPEB3 inhibits Stat5b-dependent transcription without affecting its dimerization and DNA-binding ability. (A) CPEB3 does not affect Stat5b dimerization. The 293T cells expressing flag-Stat5b and red fluorescence protein cherry (chRFP)-tagged Stat5b along with myc-CPEB3 or EGFP, were precipitated with flag Ab and probed with myc and Stat5b Abs. (B) Y699 phosphorylation in Stat5b has no effect on its dimerization as well as association with CPEB3. The 293T cells expressing myc-CPEB3 and red fluorescence protein cherry (chRFP)-tagged Stat5b along with flag-Stat5b or EGFP, were treated with or without EGF for an hour. The extracts were precipitated with flag antibody and probed with myc, Stat5b and pY699-Stat5b antibodies. (C) CPEB3 represses Stat5b-activated transcription without disrupting Stat5b’s DNA binding. The 293T cells were transfected with plasmids encoding (i) myc-CPEB3, myc-CPEB3NLS or myc-CPEB3C, and (ii) Gal4 DNA-binding domain (Gal4DBD) or Gal4DBD fused to Stat5b or FoxP2, and (iii) reporters containing firefly luciferase driven by the promoter containing five Gal4-binding sites and Renilla luciferase. The data from three sets of experiments is expressed as mean ± s.e.m. and the asterisks denote significant difference (Student’s t-test).
Figure 3. CPEB3 inhibits Stat5b-dependent transcription without affecting its dimerization and DNA-binding ability. (A) CPEB3 does not affect Stat5b dimerization. The 293T cells expressing flag-Stat5b and red fluorescence protein cherry (chRFP)-tagged Stat5b along with myc-CPEB3 or EGFP, were precipitated with flag Ab and probed with myc and Stat5b Abs. (B) Y699 phosphorylation in Stat5b has no effect on its dimerization as well as association with CPEB3. The 293T cells expressing myc-CPEB3 and red fluorescence protein cherry (chRFP)-tagged Stat5b along with flag-Stat5b or EGFP, were treated with or without EGF for an hour. The extracts were precipitated with flag antibody and probed with myc, Stat5b and pY699-Stat5b antibodies. (C) CPEB3 represses Stat5b-activated transcription without disrupting Stat5b’s DNA binding. The 293T cells were transfected with plasmids encoding (i) myc-CPEB3, myc-CPEB3NLS or myc-CPEB3C, and (ii) Gal4 DNA-binding domain (Gal4DBD) or Gal4DBD fused to Stat5b or FoxP2, and (iii) reporters containing firefly luciferase driven by the promoter containing five Gal4-binding sites and Renilla luciferase. The data from three sets of experiments is expressed as mean ± s.e.m. and the asterisks denote significant difference (Student’s t-test).CC BY-NC · PubMed Central
Figure 4. NMDAR signaling increases nuclear distribution of CPEB3. (A) Immunostaining of CPEB3 in cultured hippocampal neurons stimulated with or without NMDA for 30 min. MAP2 staining was used to identify neurons. (B) The summary result of CPEB3 localization from analyzing 500 neurons treated with various reagents for 30 min. The staining signal in the cytoplasm greater than that in the nucleus is considered as cytoplasm-localized (light gray bar) and the rest is grouped as nucleus-localized (dark gray bar). (C) The COS7 cells expressing GFP-CPEB3 were treated for 30 min with leptomycin B, fixed and stained for nuclei with Hoechst 33342. Scale: 10 µm.
Figure 4. NMDAR signaling increases nuclear distribution of CPEB3. (A) Immunostaining of CPEB3 in cultured hippocampal neurons stimulated with or without NMDA for 30 min. MAP2 staining was used to identify neurons. (B) The summary result of CPEB3 localization from analyzing 500 neurons treated with various reagents for 30 min. The staining signal in the cytoplasm greater than that in the nucleus is considered as cytoplasm-localized (light gray bar) and the rest is grouped as nucleus-localized (dark gray bar). (C) The COS7 cells expressing GFP-CPEB3 were treated for 30 min with leptomycin B, fixed and stained for nuclei with Hoechst 33342. Scale: 10 µm.CC BY-NC · PubMed Central
Figure 5. EGFR transcription is regulated by Stat5b and CPEB3. (A) The RNA levels of EGFR, CPEB3 and Stat5b in CPEB3 and Stat5b knockdown (siCPEB3 and siStat5b) hippocampal neurons were measured by quantitative RT–PCR and expressed as a relative ratio to the control knockdown (siCtrl) which was arbitrarily set to 1. The results are expressed as mean ± s.e.m. from three independent experiments and the asterisks denote the difference of statistical significance (Student’s t-test). (B) The stability of EGFR RNA in siCtrl, siCPEB3 and siStat5b neurons was measured in the presence of actinomycin D. The amount of EGFR RNA expressed as a relative ratio to the time zero siCtrl which was arbitrarily set to 1. To normalize the differential EGFR transcript level caused by CPEB3 or Stat5b knockdown, the amounts of EGFR RNA at time zero of siCPEB3 and siStat5b were arbitrarily set to 1 (normalized, siCPEB3: gray circle, siStat5b: open circle). (C) Chromatin immunoprecipitation of cortical neuronal lysate with Stat5b or control IgG. The pulled-down substances were analyzed for proteins and DNA. The Western blot shows precipitated Stat5b and the band of 190 kDa molecular weight is likely to be crosslinked dimeric Stat5b. The predicted Stat5b-binding sites within the –3000 to +300 EGFR promoter and the PCR-amplified regions (a–e) are illustrated. The specific amplified bands are indicated with asterisks. The regions, a, b and c, were amplified more evidently in the Stat5b immunoprecipitate. To increase signal intensity of the region b detected in the Stat5b immunoprecipitate, five more PCR cycles were applied. (D) Immunoblots using extracts from hippocampal neurons knocked down with CPEB2, CPEB3, CPEB4 or Stat5b. (E) Stat5b interacts with CPEB3 but not other CPEBs. The lysates containing flag-Stat5b and one of myc-tagged CPEBs1–4 were precipitated with myc Ab and probed with myc and flag Abs.
Figure 5. EGFR transcription is regulated by Stat5b and CPEB3. (A) The RNA levels of EGFR, CPEB3 and Stat5b in CPEB3 and Stat5b knockdown (siCPEB3 and siStat5b) hippocampal neurons were measured by quantitative RT–PCR and expressed as a relative ratio to the control knockdown (siCtrl) which was arbitrarily set to 1. The results are expressed as mean ± s.e.m. from three independent experiments and the asterisks denote the difference of statistical significance (Student’s t-test). (B) The stability of EGFR RNA in siCtrl, siCPEB3 and siStat5b neurons was measured in the presence of actinomycin D. The amount of EGFR RNA expressed as a relative ratio to the time zero siCtrl which was arbitrarily set to 1. To normalize the differential EGFR transcript level caused by CPEB3 or Stat5b knockdown, the amounts of EGFR RNA at time zero of siCPEB3 and siStat5b were arbitrarily set to 1 (normalized, siCPEB3: gray circle, siStat5b: open circle). (C) Chromatin immunoprecipitation of cortical neuronal lysate with Stat5b or control IgG. The pulled-down substances were analyzed for proteins and DNA. The Western blot shows precipitated Stat5b and the band of 190 kDa molecular weight is likely to be crosslinked dimeric Stat5b. The predicted Stat5b-binding sites within the –3000 to +300 EGFR promoter and the PCR-amplified regions (a–e) are illustrated. The specific amplified bands are indicated with asterisks. The regions, a, b and c, were amplified more evidently in the Stat5b immunoprecipitate. To increase signal intensity of the region b detected in the Stat5b immunoprecipitate, five more PCR cycles were applied. (D) Immunoblots using extracts from hippocampal neurons knocked down with CPEB2, CPEB3, CPEB4 or Stat5b. (E) Stat5b interacts with CPEB3 but not other CPEBs. The lysates containing flag-Stat5b and one of myc-tagged CPEBs1–4 were precipitated with myc Ab and probed with myc and flag Abs.CC BY-NC · PubMed Central
Figure 6. The kinetics of EGFR downstream signaling is altered in CPEB3-deficient hippocampal neurons. (A) The tyrosine kinase activity of EGFR as measured by autophosphorylation of Y1068 (p-Y1068) was assessed using siCtrl and siCPEB3 neurons treated with AMPA, NMDA and EGF. (B) Western blots of p-EGFR, EGFR, p-Stat5, Stat5b, p-Akt and Akt proteins in neurons treated with EGF at the indicated time. The signals were quantified and plotted against the time of treatment. The p-EGFR signal (top plot) in siCPEB3 neurons was also normalized with the fold of increase in EGFR protein level that was determined from non-EGF treated samples (normalized, gray circle). The signals of p-Stat5b at Y699 and p-Akt at T308 are displayed in the bottom plots. The signals of p-EGFR and p-Stat5b at 0.25 h and p-Akt at 0 h (i.e. no EGF treatment) from the siCtrl samples were arbitrarily set to 1. (C) Same as the above except neurons were treated with NMDA. The p-EGFR and p-Stat5b were undetectable (data not shown). The plot shows the kinetics of Akt T308 phosphorylation in siCtrl and siCPEB3 neurons.
Figure 6. The kinetics of EGFR downstream signaling is altered in CPEB3-deficient hippocampal neurons. (A) The tyrosine kinase activity of EGFR as measured by autophosphorylation of Y1068 (p-Y1068) was assessed using siCtrl and siCPEB3 neurons treated with AMPA, NMDA and EGF. (B) Western blots of p-EGFR, EGFR, p-Stat5, Stat5b, p-Akt and Akt proteins in neurons treated with EGF at the indicated time. The signals were quantified and plotted against the time of treatment. The p-EGFR signal (top plot) in siCPEB3 neurons was also normalized with the fold of increase in EGFR protein level that was determined from non-EGF treated samples (normalized, gray circle). The signals of p-Stat5b at Y699 and p-Akt at T308 are displayed in the bottom plots. The signals of p-EGFR and p-Stat5b at 0.25 h and p-Akt at 0 h (i.e. no EGF treatment) from the siCtrl samples were arbitrarily set to 1. (C) Same as the above except neurons were treated with NMDA. The p-EGFR and p-Stat5b were undetectable (data not shown). The plot shows the kinetics of Akt T308 phosphorylation in siCtrl and siCPEB3 neurons.CC BY-NC · PubMed Central
Figure 7. EGFR influences spatial memory. (A) To test gefitinib potency, the hippocampal neurons were stimulated with EGF in the presence or absence of gefitinib. The EGFR kinase activity was indicated by p-Y1068. (B) No difference in the swimming speed in the water maze task among vehicle, EGF and gefitinib-treated mice. (C) Intervention of the kinase activity of EGFR in the brain with EGF (activation) and gefitinib (inhibition) affects the learning accuracy and latency to escape in Morris water maze tasks. The accuracy was calculated per day as the trial number that the mice successfully climb onto the invisible platform divided by total four trials. The gefitinib group (n = 10) showed slower and impaired learning in Morris water maze when compared to the control vehicle group (n = 11) as judged by reduced learning accuracy (left plot, P = 0.021) and increased latency (right plot, P = 0.016) to locate the invisible platform for the four consecutive training days. In contrast, the EGF-treated group (n = 12) showed a trend of enhanced learning accuracy (left plot, P = 0.074) and decreased latency (right plot, P = 0.452). The P-value was calculated using the two-way ANOVA least square difference (LSD) analysis. (D) For the probe trial when the platform was removed after the 4-day training, the distance (left plot) and the percentage of time (right plot) that EGF- and gefitinib-treated mice swam in the target quadrant where the platform used to be were increased and reduced, respectively, when compared to the vehicle-infused mice. The P-value was calculated using the one-way ANOVA LSD test to compare the statistical difference between groups.
Figure 7. EGFR influences spatial memory. (A) To test gefitinib potency, the hippocampal neurons were stimulated with EGF in the presence or absence of gefitinib. The EGFR kinase activity was indicated by p-Y1068. (B) No difference in the swimming speed in the water maze task among vehicle, EGF and gefitinib-treated mice. (C) Intervention of the kinase activity of EGFR in the brain with EGF (activation) and gefitinib (inhibition) affects the learning accuracy and latency to escape in Morris water maze tasks. The accuracy was calculated per day as the trial number that the mice successfully climb onto the invisible platform divided by total four trials. The gefitinib group (n = 10) showed slower and impaired learning in Morris water maze when compared to the control vehicle group (n = 11) as judged by reduced learning accuracy (left plot, P = 0.021) and increased latency (right plot, P = 0.016) to locate the invisible platform for the four consecutive training days. In contrast, the EGF-treated group (n = 12) showed a trend of enhanced learning accuracy (left plot, P = 0.074) and decreased latency (right plot, P = 0.452). The P-value was calculated using the two-way ANOVA least square difference (LSD) analysis. (D) For the probe trial when the platform was removed after the 4-day training, the distance (left plot) and the percentage of time (right plot) that EGF- and gefitinib-treated mice swam in the target quadrant where the platform used to be were increased and reduced, respectively, when compared to the vehicle-infused mice. The P-value was calculated using the one-way ANOVA LSD test to compare the statistical difference between groups.CC BY-NC · PubMed Central

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Authors
Peng, S.-C., Lai, Y.-T., Huang, H.-Y., Huang, H.-D., & Huang, Y.-S.
Venue
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Published
2010-07-17
Volume
38
Issue
21
Pages
7446-7457
ISSN
  • 1362-4962
  • 0305-1048
DOI
10.1093/nar/gkq634
PMC
PMC2995057
Cited by
43
References
2
Language
en
Licence
creativecommons.org/licenses/by-nc/2.5 (vor, 2305 d)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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