ArticleThe Biochemical journal2012
The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities.
Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- Two Plasmodium vivax hypnozoite-expressed RNA-binding proteins inhibit liver stage replication.Nature communications · 2026Article
- The Link Between Serum Copper and Diabetic Kidney Disease: A Plasma Proteomic Perspective.Journal of diabetes research · 2026Article
- TwoResearch square · 2025Article
- Multifaceted roles of CARM1 beyond histone arginine methylation.Experimental & molecular medicine · 2025Review
- Participation of host cell proteins in inclusion bodies of non-segmented RNA virus infected cells: a molecular insight.Virology journal · 2025Review
- Protein phosphatase 1 suppresses PKR/EIF2α signaling during human cytomegalovirus infection.Journal of virology · 2024Article
- Targeting PRMT9-mediated arginine methylation suppresses cancer stem cell maintenance and elicits cGAS-mediated anticancer immunity.Nature cancer · 2024Article
- MAPKAP Kinase-2 phosphorylation of PABPC1 controls its interaction with 14-3-3 proteins after DNA damage: A combined kinase and protein array approach.Frontiers in molecular biosciences · 2023Article
- Dual Leucine Zipper Kinase Regulates Dscam Expression through a Noncanonical Function of the Cytoplasmic Poly(A)-Binding Protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- The molecular basis of coupling between poly(A)-tail length and translational efficiency.eLife · 2021Article
- Musashi interaction with poly(A)-binding protein is required for activation of target mRNA translation.The Journal of biological chemistry · 2019Article
- Phosphorylation and interactions associated with the control of the Leishmania Poly-A Binding Protein 1 (PABP1) function during translation initiation.RNA biology · 2018Article
- The C-Terminal RGG Domain of Human Lsm4 Promotes Processing Body Formation Stimulated by Arginine Dimethylation.Molecular and cellular biology · 2016Article
- Bovine Adenovirus-3 pVIII Suppresses Cap-Dependent mRNA Translation Possibly by Interfering with the Recruitment of DDX3 and Translation Initiation Factors to the mRNA Cap.Frontiers in microbiology · 2016Article
- The complexity of miRNA-mediated repression.Cell death and differentiation · 2015Review
- The role of the poly(A) binding protein in the assembly of the Cap-binding complex during translation initiation in plants.Translation (Austin, Tex.) · 2014Review
- The RNA binding domain of Pumilio antagonizes poly-adenosine binding protein and accelerates deadenylation.RNA (New York, N.Y.) · 2014Article
- Emerging roles for ribonucleoprotein modification and remodeling in controlling RNA fate.Trends in cell biology · 2013Review
- Phosphorylation at intrinsically disordered regions of PAM2 motif-containing proteins modulates their interactions with PABPC1 and influences mRNA fate.RNA (New York, N.Y.) · 2013Article
- Control of translation and miRNA-dependent repression by a novel poly(A) binding protein, hnRNP-Q.PLoS biology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
PABP1 [poly(A)-binding protein 1] is a central regulator of mRNA translation and stability and is required for miRNA (microRNA)-mediated regulation and nonsense-mediated decay. Numerous protein, as well as RNA, interactions underlie its multi-functional nature; however, it is unclear how its different activities are co-ordinated, since many partners interact via overlapping binding sites. In the present study, we show that human PABP1 is subject to elaborate post-translational modification, identifying 14 modifications located throughout the functional domains, all but one of which are conserved in mouse. Intriguingly, PABP1 contains glutamate and aspartate methylations, modifications of unknown function in eukaryotes, as well as lysine and arginine methylations, and lysine acetylations. The latter dramatically alter the pI of PABP1, an effect also observed during the cell cycle, suggesting that different biological processes/stimuli can regulate its modification status, although PABP1 also probably exists in differentially modified subpopulations within cells. Two lysine residues were differentially acetylated or methylated, revealing that PABP1 may be the first example of a cytoplasmic protein utilizing a 'methylation/acetylation switch'. Modelling using available structures implicates these modifications in regulating interactions with individual PAM2 (PABP-interacting motif 2)-containing proteins, suggesting a direct link between PABP1 modification status and the formation of distinct mRNP (messenger ribonucleoprotein) complexes that regulate mRNA fate in the cytoplasm.
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