Poly(A) binding proteins: are they all created equal?

Goss, Dixie J.; Kleiman, Frida E.

doi:10.1002/wrna.1151

Cited by 114 publications

(102 citation statements)

References 131 publications

(168 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The capbinding translation initiation complex eIF4F serves to promote translation initiation, while preventing access to the mRNA cap for the DCP2 decapping complex (von der Haar et al 2004). Cytoplasmic poly(A)-binding protein (PABPC) stimulates translation initiation while impacting mRNA deadenylation through repression or stimulation of deadenylase complexes (Goss and Kleiman 2013). Consistent with this relation between translation initiation and mRNA stability, many RNA-binding proteins (RBPs) that promote mRNA degradation also repress translation initiation (Wharton et al 1998;Pillai et al 2004;Pfeiffer and Brooks 2012).…”

Section: Introductionmentioning

confidence: 95%

Recruitment of the 4EHP-GYF2 cap-binding complex to tetraproline motifs of tristetraprolin promotes repression and degradation of mRNAs with AU-rich elements

Olsen

Webb

et al. 2016

RNA

101

View full text Add to dashboard Cite

The zinc finger protein tristetraprolin (TTP) promotes translation repression and degradation of mRNAs containing AU-rich elements (AREs). Although much attention has been directed toward understanding the decay process and machinery involved, the translation repression role of TTP has remained poorly understood. Here we identify the cap-binding translation repression 4EHP-GYF2 complex as a cofactor of TTP. Immunoprecipitation and in vitro pull-down assays demonstrate that TTP associates with the 4EHP-GYF2 complex via direct interaction with GYF2, and mutational analyses show that this interaction occurs via conserved tetraproline motifs of TTP. Mutant TTP with diminished 4EHP-GYF2 binding is impaired in its ability to repress a luciferase reporter ARE-mRNA. 4EHP knockout mouse embryonic fibroblasts (MEFs) display increased induction and slower turnover of TTP-target mRNAs as compared to wild-type MEFs. Our work highlights the function of the conserved tetraproline motifs of TTP and identifies 4EHP-GYF2 as a cofactor in translational repression and mRNA decay by TTP.

show abstract

Section: Introductionmentioning

confidence: 95%

Recruitment of the 4EHP-GYF2 cap-binding complex to tetraproline motifs of tristetraprolin promotes repression and degradation of mRNAs with AU-rich elements

Olsen

Webb

et al. 2016

RNA

101

View full text Add to dashboard Cite

show abstract

“…In mammals, PABPs have extensive roles in the nucleus and cytoplasm in mRNA processing, translation and degradation, as well as a role in miRNA-mediated processes (reviewed in Goss and Kleiman, 2013). Higher eukaryotes have multiple genes for PABP.…”

Section: Poly(a) Binding Proteinmentioning

confidence: 99%

Mechanism of Cytoplasmic mRNA Translation

Browning

Bailey‐Serres

2015

The Arabidopsis Book

186

220

View full text Add to dashboard Cite

Protein synthesis is a fundamental process in gene expression that depends upon the abundance and accessibility of the mRNA transcript as well as the activity of many protein and RNA-protein complexes. Here we focus on the intricate mechanics of mRNA translation in the cytoplasm of higher plants. This chapter includes an inventory of the plant translational apparatus and a detailed review of the translational processes of initiation, elongation, and termination. The majority of mechanistic studies of cytoplasmic translation have been carried out in yeast and mammalian systems. The factors and mechanisms of translation are for the most part conserved across eukaryotes; however, some distinctions are known to exist in plants. A comprehensive understanding of the complex translational apparatus and its regulation in plants is warranted, as the modulation of protein production is critical to development, environmental plasticity and biomass yield in diverse ecosystems and agricultural settings.

show abstract

“…Human polyadenylate-binding proteins (PABPs) belong to a conserved protein family that binds to the poly(A) tail of mRNA through RRMs (Goss and Kleiman 2013). Six PABP paralogs in humans (PABP1, PABP3, PABP4, PABP5, PAP1L, and PAP4L) contain four RRM domains, with some members containing an additional C-terminal domain called PABC.…”

Section: Ancient Rrm Duplications In Pabpsmentioning

confidence: 99%

Prevalent RNA recognition motif duplication in the human genome

Tsai¹,

Gomez

Wang

2014

RNA

View full text Add to dashboard Cite

The sequence-specific recognition of RNA by proteins is mediated through various RNA binding domains, with the RNA recognition motif (RRM) being the most frequent and present in >50% of RNA-binding proteins (RBPs). Many RBPs contain multiple RRMs, and it is unclear how each RRM contributes to the binding specificity of the entire protein. We found that RRMs within the same RBP (i.e., sibling RRMs) tend to have significantly higher similarity than expected by chance. Sibling RRM pairs from RBPs shared by multiple species tend to have lower similarity than those found only in a single species, suggesting that multiple RRMs within the same protein might arise from domain duplication followed by divergence through random mutations. This finding is exemplified by a recent RRM domain duplication in DAZ proteins and an ancient duplication in PABP proteins. Additionally, we found that different similarities between sibling RRMs are associated with distinct functions of an RBP and that the RBPs tend to contain repetitive sequences with low complexity. Taken together, this study suggests that the number of RBPs with multiple RRMs has expanded in mammals and that the multiple sibling RRMs may recognize similar target motifs in a cooperative manner.

show abstract

Poly(A) binding proteins: are they all created equal?

Cited by 114 publications

References 131 publications

Recruitment of the 4EHP-GYF2 cap-binding complex to tetraproline motifs of tristetraprolin promotes repression and degradation of mRNAs with AU-rich elements

Recruitment of the 4EHP-GYF2 cap-binding complex to tetraproline motifs of tristetraprolin promotes repression and degradation of mRNAs with AU-rich elements

Mechanism of Cytoplasmic mRNA Translation

Prevalent RNA recognition motif duplication in the human genome

Contact Info

Product

Resources

About