Cited by 127RNA Research and SplicingRNA and protein synthesis mechanismsRNA regulation and disease

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

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Goss, Dixie J., Kleiman, Frida Esther·2013·WIREs RNA

Abstract

The PABP family of proteins were originally thought of as a simple shield for the mRNA poly(A) tail. Years of research have shown that PABPs interact not only with the poly(A) tail, but also with specific sequences in the mRNA, having a general and specific role on the metabolism of different mRNAs. The complexity of PABPs function is increased by the interactions of PABPs with factors involved in different cellular functions. PABPs participate in all the metabolic pathways of the mRNA: polyadenylation/deadenylation, mRNA export, mRNA surveillance, translation, mRNA degradation, microRNA‐associated regulation, and regulation of expression during development. In this review, we update information on the roles of PABPs and emerging data on the specific interactions of PABP homologs. Specific functions of individual members of PABPC family in development and viral infection are beginning to be elucidated. However, the interactions are complex and recent evidence for exchange of nuclear and cytoplasmic forms of the proteins, as well as post‐translational modifications, emphasize the possibilities for fine‐tuning the PABP metabolic network. WIREs RNA 2013, 4:167–179. doi: 10.1002/wrna.1151 This article is categorized under: RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications Translation > Translation Regulation RNA Processing > 3' End Processing

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  • The poly(A) tail can bind to multiple poly(A)-binding proteins (PABPs) while working synergistically with 5′ m7G cap sequences to regulate translational efficiency.

    “The poly(A) tail can also bind to multiple poly(A)-binding proteins (PABPs) while working synergistically with 5′ m7G cap sequences to regulate translational efficiency.146,147”

    From Advances in COVID-19 mRNA vaccine development (2022) · cites this paper as [146]

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Authors
Goss, D. J., & Kleiman, F. E.
Affiliations
Hunter College (US)
Corresponding author
Goss, Dixie J.
Venue
WIREs RNA
Publisher
Wiley
Published
2012-12-13
Volume
4
Issue
2
Pages
167-179
ISSN
  • 1757-7004 (ISSN-L)
  • 1757-7012
OpenAlex
W2074396001
Cited by
127
References
131
Citations by year
2026: 2 · 2025: 2 · 2024: 14 · 2023: 13 · 2022: 13 · 2021: 12 · 2020: 18 · 2019: 6 · 2018: 13 · 2017: 5 · 2016: 6 · 2015: 9 · 2014: 12 · 2013: 2
FWCI
0.67
Type
journal article
Language
en
Open access
Locations
  • Wiley Interdisciplinary Reviews - RNA (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Science Foundation
  • National Institute of General Medical Sciences (SC1GM083806)
  • National Center for Research Resources (G12RR003037)
  • National Institute on Minority Health and Health Disparities (G12MD007599)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
Keywords
poly(A)-binding protein, poly(A) tail, mRNA polyadenylation, mRNA deadenylation, mRNA export, mRNA surveillance, translational regulation, mRNA degradation, microRNA regulation, post-translational modification, viral infection, development (biology)
MeSH terms
Animals, Multigene Family, Humans, Protein Binding, RNA, Messenger, Virus Diseases, Poly(A)-Binding Proteins

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