IndraLab

Statements

PAN3 affects PAN2
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PAN3 binds PAN2.
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PAN2 binds PAN3. 10 / 327
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"In humans, TNRC6C also independently interacts with the PAN2 and PAN3 complex and contributes to gene silencing by miRNA."
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"Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation."
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"This binding allows Pan3 to supply Pan2 with substrate polyA RNA, facilitating efficient mRNA deadenylation by the intact Pan2 and Pan3 complex."
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"The mechanism of Pan2 and Pan3 complex formation and substrate binding remain elusive."
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"Recent work showed that Pan3 forms a homodimer in solution (Christie etal, 2013) raising the question of whether the Pan2 and Pan3 complex contains one or two exonuclease subunits."
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"The poly (A) tail degrading enzyme Pan2-Pan3 complex has been reported to be inhibited by Pbp1 [ xref ]."
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"To examine whether the Pan2-Pan3 complex controls COX10 , COX11 , and AIM33 mRNA, we prepared the pbp1Δ pan2Δ double mutant and then performed qRT-PCR analysis."
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"These results suggest that Pbp1 does not regulate the expression of COX10 , COX11 , and AIM33 mRNAs through the Pan2-Pan3 complex."
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"From the above results, Pbp1 can stabilize COX10 , COX11 , and AIM33 mRNAs by inhibiting decapping factors rather than acting on deadenylases, the Ccr4-Not and Pan2-Pan3 complexes."
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"Two other Drosophila poly(A)-specific ribonucleases, the Pan2-Pan3 complex and the poly(A)-specific ribonuclease (PARN), have both specialized and redundant functions when compared to the CCR4-NOT com[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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PAN3 binds CNOT7, PAN2, and ccr4. 5 / 5
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"The notion that the Pan2–Pan3 and Ccr4–Caf1 complexes can associate with each other was further confirmed by the results showing that Pan3-V5, endogenous Caf1, and a modest amount of endogenous PABP were coprecipitated with HA-Pan2 by an anti-HA antibody when HA-Pan2 and Pan3-V5 were coexpressed ( xref )."
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"Since ARE/ARE-BP complexes have not yet been reported to directly interact with either the Pan2-Pan3 or Ccr4-Caf1 complex, one possibility is that the binding of ARE-BPs to AREs may interfere with the interaction between the 5′ cap/eIF4F complex and the 3′ poly(A)/PABP complex, thus preventing the formation of a closed-loop structure ( xref )."
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"Although Pan3 and Caf1 associate with Pan2 and Ccr4 poly(A) nucleases, respectively ( xref ; xref ; xref ; xref ; xref ), their in vivo roles in mammalian mRNA turnover remain unclear."
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"Pan2–Pan3 and Ccr4–Caf1 complexes can interact with each other in vivo."
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"Additionally, Pan2-Pan3 can form a super complex with Ccr4-Caf1, which provides an opportunity to coordinate the two phases of deadenylation [ xref ]."
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PAN3 binds PAN2 and PABP. 1 / 1
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"Thus, where the Pan2-Pan3 complex can interact directly with the PABP, this interaction is indirect in case of the Ccr4-Not complex."
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PAN3 binds PAN2 and PKC. 1 / 1
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"When we tested the interaction of the ct Pan2–Pan3 PKC complex with polyA RNA, the binding was comparable to ct Pan3 PKC alone (Fig  xref B)."
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PAN3 binds PAN2 and ccr4. 1 / 1
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"Interestingly, interactions between Pan2-Pan3 and Ccr4-Not can be detected suggesting that both deadenylase complexes can reside in a higher order complex that may include other components ( xref )."
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MARF1 binds PAN2 and PAN3. 1 / 1
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"Next, we tested whether MARF1 binds Pan2 and Pan3, components of the Pan2–Pan3 deadenylase complex, and found that they did not co-immunoprecipitate with MARF1 (Supplementary Fig.  xref , D)."
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Ccr4 binds PAN3, PAN2, and exonuclease. 1 / 1
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"Of note, Ago2 is also known to regulate mRNA silencing through interacting with exonuclease complexes, the Ccr4-Not and Pan2-Pan3 complexes xref , in a miRNA-independent manner, which likely contributes to suppression of protein translation and energy metabolism in the liver."
30201950
MTA2 binds PAN3 and PAN2. 1 / 1
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"In summary, we found that it was difficult to disrupt the Pan2–Pan3 interaction by deletion of substantial regions of ct Pan2 PID and show that a core region (residues 343–406) makes a major contribution to the association of ct Pan2 and ct Pan3."
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PAN3 binds PAN2 and RNPC3. 1 / 1
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"We concluded that Pan2-Pan3 does not stably interact with short poly(A) RNPs containing a single Pab1 but requires longer poly(A) RNPs containing two or more Pab1 protomers."
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PAN3 binds PAN2, CNOT7, ccr4, and Nuclease. 1 / 1
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"Collectively, our data support that Pan2–Pan3 and Ccr4–Caf1 poly(A) nuclease complexes can associate with each other to form a supercomplex in vivo."
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PAN3 inhibits PAN2.
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PAN3 inhibits PAN2. 1 / 2
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"It is therefore a possibility that PAN3 depletion prevents USP52 localization to P-bodies and thus contributes to the destabilization of AMD substrates, as we have observed in the case of HIF1A."
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PAN3 activates PAN2.
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PAN3 activates PAN2. 2 / 2
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"Instead, Pan3 may modulate the activity of Pan2 poly (A) nuclease or link deadenylation to subsequent decay of the mRNA body."
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"Because Pan3 is able to enhance localization of Pan2 to P-bodies (XREF_FIG), we then tested whether Pan3 also helps Ccr4 and Caf1 localize to P-bodies."
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CNOT7 affects ETF1, PAN2, PAN3, ccr4, and eRF3
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ERF3 binds ETF1, PAN3, PAN2, ccr4, and CNOT7. 2 / 2
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"Interestingly, translation termination complexes eRF1-eRF3, Pan2-Pan3, and Caf1-Ccr4 competitively interact with polyadenylate-binding protein PABPC1."
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"Recent studies showed that translation termination complexes eRF1–eRF3, Pan2–Pan3, and Caf1–Ccr4 competitively bind to PABPC1via the PAM2 motifs of eRF3, Pan3, and Tob."
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Exonuclease affects ccr4
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Ccr4 binds PAN3, PAN2, and exonuclease. 1 / 1
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"Of note, Ago2 is also known to regulate mRNA silencing through interacting with exonuclease complexes, the Ccr4-Not and Pan2-Pan3 complexes xref , in a miRNA-independent manner, which likely contributes to suppression of protein translation and energy metabolism in the liver."
30201950
Ccr4 affects Nuclease
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PAN3 binds PAN2, CNOT7, ccr4, and Nuclease. 1 / 1
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"Collectively, our data support that Pan2–Pan3 and Ccr4–Caf1 poly(A) nuclease complexes can associate with each other to form a supercomplex in vivo."
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RNPC3 affects PAN3
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PAN3 binds PAN2 and RNPC3. 1 / 1
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"We concluded that Pan2-Pan3 does not stably interact with short poly(A) RNPs containing a single Pab1 but requires longer poly(A) RNPs containing two or more Pab1 protomers."
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PKC affects PAN3
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PAN3 binds PAN2 and PKC. 1 / 1
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"When we tested the interaction of the ct Pan2–Pan3 PKC complex with polyA RNA, the binding was comparable to ct Pan3 PKC alone (Fig  xref B)."
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PAN3 affects exonuclease
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Ccr4 binds PAN3, PAN2, and exonuclease. 1 / 1
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"Of note, Ago2 is also known to regulate mRNA silencing through interacting with exonuclease complexes, the Ccr4-Not and Pan2-Pan3 complexes xref , in a miRNA-independent manner, which likely contributes to suppression of protein translation and energy metabolism in the liver."
30201950
PAN3 affects RNPC3
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PAN3 binds PAN2 and RNPC3. 1 / 1
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"We concluded that Pan2-Pan3 does not stably interact with short poly(A) RNPs containing a single Pab1 but requires longer poly(A) RNPs containing two or more Pab1 protomers."
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PAN3 affects PKC
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PAN3 binds PAN2 and PKC. 1 / 1
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"When we tested the interaction of the ct Pan2–Pan3 PKC complex with polyA RNA, the binding was comparable to ct Pan3 PKC alone (Fig  xref B)."
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PAN3 affects PABP
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PAN3 binds PAN2 and PABP. 1 / 1
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"Thus, where the Pan2-Pan3 complex can interact directly with the PABP, this interaction is indirect in case of the Ccr4-Not complex."
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PAN3 affects Nuclease
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PAN3 binds PAN2, CNOT7, ccr4, and Nuclease. 1 / 1
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"Collectively, our data support that Pan2–Pan3 and Ccr4–Caf1 poly(A) nuclease complexes can associate with each other to form a supercomplex in vivo."
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PAN3 affects MTA2
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MTA2 binds PAN3 and PAN2. 1 / 1
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"In summary, we found that it was difficult to disrupt the Pan2–Pan3 interaction by deletion of substantial regions of ct Pan2 PID and show that a core region (residues 343–406) makes a major contribution to the association of ct Pan2 and ct Pan3."
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PAN3 affects MARF1
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MARF1 binds PAN2 and PAN3. 1 / 1
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"Next, we tested whether MARF1 binds Pan2 and Pan3, components of the Pan2–Pan3 deadenylase complex, and found that they did not co-immunoprecipitate with MARF1 (Supplementary Fig.  xref , D)."
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PAN2 affects exonuclease
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Ccr4 binds PAN3, PAN2, and exonuclease. 1 / 1
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"Of note, Ago2 is also known to regulate mRNA silencing through interacting with exonuclease complexes, the Ccr4-Not and Pan2-Pan3 complexes xref , in a miRNA-independent manner, which likely contributes to suppression of protein translation and energy metabolism in the liver."
30201950
PAN2 affects RNPC3
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PAN3 binds PAN2 and RNPC3. 1 / 1
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"We concluded that Pan2-Pan3 does not stably interact with short poly(A) RNPs containing a single Pab1 but requires longer poly(A) RNPs containing two or more Pab1 protomers."
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PAN2 affects PKC
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PAN3 binds PAN2 and PKC. 1 / 1
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"When we tested the interaction of the ct Pan2–Pan3 PKC complex with polyA RNA, the binding was comparable to ct Pan3 PKC alone (Fig  xref B)."
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PAN2 affects PAN3, ccr4, and exonuclease
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Ccr4 binds PAN3, PAN2, and exonuclease. 1 / 1
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"Of note, Ago2 is also known to regulate mRNA silencing through interacting with exonuclease complexes, the Ccr4-Not and Pan2-Pan3 complexes xref , in a miRNA-independent manner, which likely contributes to suppression of protein translation and energy metabolism in the liver."
30201950
PAN2 affects PAN3, and ccr4
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PAN3 binds PAN2 and ccr4. 1 / 1
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"Interestingly, interactions between Pan2-Pan3 and Ccr4-Not can be detected suggesting that both deadenylase complexes can reside in a higher order complex that may include other components ( xref )."
24391663
PAN2 affects PAN3, and RNPC3
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PAN3 binds PAN2 and RNPC3. 1 / 1
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"We concluded that Pan2-Pan3 does not stably interact with short poly(A) RNPs containing a single Pab1 but requires longer poly(A) RNPs containing two or more Pab1 protomers."
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PAN2 affects PAN3, and PKC
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PAN3 binds PAN2 and PKC. 1 / 1
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"When we tested the interaction of the ct Pan2–Pan3 PKC complex with polyA RNA, the binding was comparable to ct Pan3 PKC alone (Fig  xref B)."
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PAN2 affects PABP
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PAN3 binds PAN2 and PABP. 1 / 1
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"Thus, where the Pan2-Pan3 complex can interact directly with the PABP, this interaction is indirect in case of the Ccr4-Not complex."
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PAN2 affects Nuclease
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PAN3 binds PAN2, CNOT7, ccr4, and Nuclease. 1 / 1
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"Collectively, our data support that Pan2–Pan3 and Ccr4–Caf1 poly(A) nuclease complexes can associate with each other to form a supercomplex in vivo."
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PAN2 affects MTA2
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MTA2 binds PAN3 and PAN2. 1 / 1
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"In summary, we found that it was difficult to disrupt the Pan2–Pan3 interaction by deletion of substantial regions of ct Pan2 PID and show that a core region (residues 343–406) makes a major contribution to the association of ct Pan2 and ct Pan3."
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PAN2 affects MARF1
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MARF1 binds PAN2 and PAN3. 1 / 1
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"Next, we tested whether MARF1 binds Pan2 and Pan3, components of the Pan2–Pan3 deadenylase complex, and found that they did not co-immunoprecipitate with MARF1 (Supplementary Fig.  xref , D)."
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PABP affects PAN3
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PAN3 binds PAN2 and PABP. 1 / 1
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"Thus, where the Pan2-Pan3 complex can interact directly with the PABP, this interaction is indirect in case of the Ccr4-Not complex."
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Nuclease affects ccr4
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PAN3 binds PAN2, CNOT7, ccr4, and Nuclease. 1 / 1
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"Collectively, our data support that Pan2–Pan3 and Ccr4–Caf1 poly(A) nuclease complexes can associate with each other to form a supercomplex in vivo."
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MTA2 affects PAN3
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MTA2 binds PAN3 and PAN2. 1 / 1
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"In summary, we found that it was difficult to disrupt the Pan2–Pan3 interaction by deletion of substantial regions of ct Pan2 PID and show that a core region (residues 343–406) makes a major contribution to the association of ct Pan2 and ct Pan3."
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MARF1 affects PAN3
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MARF1 binds PAN2 and PAN3. 1 / 1
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"Next, we tested whether MARF1 binds Pan2 and Pan3, components of the Pan2–Pan3 deadenylase complex, and found that they did not co-immunoprecipitate with MARF1 (Supplementary Fig.  xref , D)."
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CNOT7 affects Nuclease, PAN2, PAN3, and ccr4
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PAN3 binds PAN2, CNOT7, ccr4, and Nuclease. 1 / 1
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"Collectively, our data support that Pan2–Pan3 and Ccr4–Caf1 poly(A) nuclease complexes can associate with each other to form a supercomplex in vivo."
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