Abstract
RNA-binding proteins are of vital importance for mRNA functioning. Among these, poly(A)-binding proteins (PABPs) are of special interest due to their participation in virtually all mRNA-dependent events that is caused by their high affinity for A-rich mRNA sequences. Apart from mRNAs, PABPs interact with many proteins, thus promoting their involvement in cellular events. In the nucleus, PABPs play a role in polyadenylation, determine the length of the poly(A) tail, and may be involved in mRNA export. In the cytoplasm, they participate in regulation of translation initiation and either protect mRNAs from decay through binding to their poly(A) tails or stimulate this decay by promoting mRNA inter-actions with deadenylase complex proteins. This review presents modern notions of the role of PABPs in mRNA-dependent events; peculiarities of regulation of PABP amount in the cell and activities are also discussed.
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Abbreviations
- ARE:
-
AU-rich element
- ARS:
-
adenine-rich autoregulatory sequence
- Cp:
-
ceruloplasmin
- CPE:
-
cytoplasmic polyadenylation element
- CPEBP:
-
cytoplasmic polyadenylation element binding protein
- CPSF:
-
cleavage and polyadenylation specificity factor
- eIF:
-
eukaryotic initiation factor
- EJC:
-
exon junction complex
- eRF:
-
eukaryotic release factor
- GAIT-element:
-
interferon γ-activated inhibitor of translation
- hnRNP:
-
heterogeneous nuclear ribonucleoprotein
- IFN-γ:
-
interferon γ
- IRES:
-
internal ribosome entry site
- MLLE:
-
C-terminal domain of PABP
- Msi1:
-
Musashi 1
- NMD:
-
nonsense mediated mRNA decay
- PABPs:
-
poly(A)-binding proteins
- Paip1/2:
-
PABP-interacting protein 1/2
- PAM:
-
PABP-interacting motif
- PAN2/3:
-
PABP-dependent poly(A)-specific ribonuclease 2/3
- PAP:
-
poly(A) polymerase
- PARN:
-
poly(A)-specific ribonuclease
- PTC:
-
premature termination codon
- RRM:
-
RNA recognition motif
- TOP:
-
terminal oligopyrimidine track
- UNR:
-
upstream of N-ras
- UTR:
-
untranslated region
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Published in Russian in Uspekhi Biologicheskoi Khimii, 2013, Vol. 53, pp. 3–34.
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Eliseeva, I.A., Lyabin, D.N. & Ovchinnikov, L.P. Poly(A)-binding proteins: Structure, domain organization, and activity regulation. Biochemistry Moscow 78, 1377–1391 (2013). https://doi.org/10.1134/S0006297913130014
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DOI: https://doi.org/10.1134/S0006297913130014