Poly(A) Nuclease Interacts with the C-terminal Domain of Polyadenylate-binding Protein Domain from Poly(A)-binding Protein

Siddiqui, Nadeem; Mangus, David A.; Chang, Tsung Cheng; Palermino, Jeanne Marie; Shyu, Ann‐Bin; Gehring, Kalle

doi:10.1074/jbc.m701256200

Cited by 83 publications

(77 citation statements)

References 58 publications

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“…2b). These results suggest that PAN2-PAN3 is primarily recruited through the function of W-motifs but that it can also weakly interact with the CED through PABP, which is consistent with the direct PAN3-PABP interaction previously described 20 .…”

Section: W-motifs Represent Signals Recruiting Deadenylase Complexessupporting

confidence: 77%

miRNA repression involves GW182-mediated recruitment of CCR4–NOT through conserved W-containing motifs

Chekulaeva

Mathys

Zipprich

et al. 2011

Nat Struct Mol Biol

326

449

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AbstractmiRNA-mediated repression in animals is dependent on the GW182 protein family. GW182 proteins are recruited to the miRNA repression complex through direct interaction with Argonaute proteins, and they function downstream to repress target mRNA. Here we demonstrate that in human and Drosophila melanogaster cells, the critical repressive features of both the N-terminal and C-terminal effector domains of GW182 proteins are Gly/Ser/Thr-Trp (G/S/TW) or Trp-Gly/ Ser/Thr (WG/S/T) motifs. These motifs, which are dispersed across both domains and act in an additive manner, function by recruiting components of the CCR 4-NOT deadenylation complex. A heterologous yeast polypeptide with engineered WG/S/T motifs acquired the ability to repress tethered mRNA and to interact with the CCR 4-NOT complex. These results identify previously unknown effector motifs functioning as important mediators of miRNA-induced silencing in both species, and they reveal that recruitment of the CCR 4-NOT complex by tryptophan-containing motifs acts downstream of GW182 to repress mRNA s, including inhibiting translation independently of deadenylation.MicroRNAs (miRNAs) are small, ~21-nt-long RNAs that post-transcriptionally regulate gene expression in eukaryotes. In animals, miRNAs bind to partially complementary sites in mRNAs, leading to translational repression and mRNA deadenylation and degradation [1][2][3][4] . miRNAs function as part of ribonucleoprotein complexes, miRNPs, with Argonaute (AGO) and GW182 family proteins being the crucial components. GW182s interact directly with AGO proteins and function downstream as effectors mediating mRNA repression. Hence, understanding the function of GW182 proteins is critical for understanding miRNAmediated repression.GW182 functional regions have been mapped in D. melanogaster and mammalian proteins. In D. melanogaster, three regions were found to repress tethered mRNA to a similar extent 5

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Section: W-motifs Represent Signals Recruiting Deadenylase Complexessupporting

confidence: 77%

miRNA repression involves GW182-mediated recruitment of CCR4–NOT through conserved W-containing motifs

Chekulaeva

Mathys

Zipprich

et al. 2011

Nat Struct Mol Biol

326

449

View full text Add to dashboard Cite

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“…Phenylalanine residues play a major role in PAM2-PABC/MLLE recognition (Siddiqui et al 2007) so positions F92, F104, and F117 were targeted, and also other positions conserved in an alignment of eRF3 sequences from yeast species (data not shown). Only mutations of phenylalanine residues diminished eRF3 interaction with Pab1 ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…This motif is found in PABP partners in different organisms except in yeast. Of the three factors that interact with Pab1-C-terminal domain in yeast; eRF3, Pan3, and Pbp1, only Pan3 contains a PAM2 motif (Mangus et al 1998;Siddiqui et al 2007;). Structures of PABC/MLLE have been obtained and the one from yeast is divergent (Kozlov et al 2002).…”

Section: Discussionmentioning

confidence: 99%

Interaction between the poly(A)-binding protein Pab1 and the eukaryotic release factor eRF3 regulates translation termination but not mRNA decay in Saccharomyces cerevisiae

Roque

Cerciat

Gaugué

et al. 2014

RNA

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Eukaryotic release factor 3 (eRF3) is implicated in translation termination and also interacts with the poly(A)-binding protein (PABP, Pab1 in yeast), a major player in mRNA metabolism. Despite conservation of this interaction, its precise function remains elusive. First, we showed experimentally that yeast eRF3 does not contain any obvious consensus PAM2 (PABP-interacting motif 2). Thus, in yeast this association is different from the well described interaction between the metazoan factors. To gain insight into the exact function of this interaction, we then analyzed the phenotypes resulting from deleting the respective binding domains. Deletion of the Pab1 interaction domain on eRF3 did not affect general mRNA stability or nonsense-mediated mRNA decay (NMD) pathway and induced a decrease in translational readthrough. Furthermore, combined deletions of the respective interacting domains on eRF3 and on Pab1 were viable, did not affect Pab1 function in mRNA stability and harbored an antisuppression phenotype. Our results show that in Saccharomyces cerevisiae the role of the Pab1 C-terminal domain in mRNA stability is independent of eRF3 and the association of these two factors negatively regulates translation termination.

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“…FBPase activity is indirectly regulated by cAMP, which increases in vivo in the kidney epithelia exposed to fructose compared with those exposed to glucose. It has been demonstrated in vivo that cAMP modulates fructose transport induced by fructose without affecting GLUT5 mRNA abundance (65), whereas in vitro, cAMP affects GLUT5 mRNA expression levels and is involved in GLUT5 regulation in kidney epithelia (67)(68)(69)(70).…”

Section: Discussionmentioning

confidence: 99%

Fructose transporter Glut5 expression in clear renal cell carcinoma

Villaamil

Gallego²,

Rubira³

et al. 2011

Oncol Rep

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Abstract. Renal cell carcinomas (RCC) can be subclassified for general purposes into clear cell, papillary cell, chromophobe cell carcinomas and oncocytomas. Other tumours such as collecting duct, medullary, mucinous tubular and spindle cell and associated with Xp 11.2 translocations/TFE 3 gene fusion, are much less common. There is also a residual group of unclassified cases. Previous studies have shown that RCC has high glycolytic rates, and expresses GLUT transporters, but no distinction has been made among the different subtypes of renal cell tumours and their grades of malignancy. In clear renal cell carcinoma (cRCC) glycogen levels increase, glycolysis is activated and gluconeogenesis is reduced. The clear cell subtype of RCC is characterized histologically by a distinctive pale, glassy cytoplasm and this appearance of cRCC is due to abnormalities in carbohydrate and lipid metabolism, and this abnormality results in glycogen and sterol storage. Several isoforms of glucose carriers (GLUTs) have been identified. We show here in a panel of 80 cRCC samples a significant correlation between isoform 5 (GLUT5) and many pathological parameters such as grade of differentiation, pelvis invasion and breaking capsule. GLUT5 expression also appears to associate more strongly with the clear cell RCC subtype. These data suggest a role for the GLUT5 isoform in fructose uptake that takes place in cRCC cells and which subsequently leads to the malignant RCC progression.

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Poly(A) Nuclease Interacts with the C-terminal Domain of Polyadenylate-binding Protein Domain from Poly(A)-binding Protein

Cited by 83 publications

References 58 publications

miRNA repression involves GW182-mediated recruitment of CCR4–NOT through conserved W-containing motifs

miRNA repression involves GW182-mediated recruitment of CCR4–NOT through conserved W-containing motifs

Interaction between the poly(A)-binding protein Pab1 and the eukaryotic release factor eRF3 regulates translation termination but not mRNA decay in Saccharomyces cerevisiae

Fructose transporter Glut5 expression in clear renal cell carcinoma

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