Importin α-Mediated Nuclear Import of Cytoplasmic Poly(A) Binding Protein Occurs as a Direct Consequence of Cytoplasmic mRNA Depletion
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Recent studies have found the cytoplasmic poly(A) binding protein (PABPC) to have opposing effects on gene expression when concentrated in the cytoplasm versus in the nucleus. PABPC is predominantly cytoplasmic at steady state, where it enhances protein synthesis through simultaneous interactions with mRNA and translation factors. However, it accumulates dramatically within the nucleus in response to various pathogenic and nonpathogenic stresses, leading to an inhibition of mRNA export. The molecular events that trigger relocalization of PABPC and the mechanisms by which it translocates into the nucleus to block gene expression are not understood. Here, we reveal an RNA-based mechanism of retaining PABPC in the cytoplasm. Expression either of viral proteins that promote mRNA turnover or of a cytoplasmic deadenylase drives nuclear relocalization of PABPC in a manner dependent on the PABPC RNA recognition motifs (RRMs). Using multiple independent binding sites within its RRMs, PABPC interacts with importin α, a component of the classical import pathway. Finally, we demonstrate that the direct association of PABPC with importin α is antagonized by the presence of poly(A) RNA, supporting a model in which RNA binding masks nuclear import signals within the PABPC RRMs, thereby ensuring efficient cytoplasmic retention of this protein in normal cells. These findings further suggest that cells must carefully calibrate the ratio of PABPC to mRNA, as events that offset this balance can dramatically influence gene expression.
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The UV-dependent regulation of XPA-importin-α4 binding is probably through association with other cytoplasmic factors that may mask the XPA NLS.
“probably through the association with other cytoplasmic factors that may mask the XPA NLS [48] [49].”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [48]
The lack of efficient recognition of the XPA NLS by importin-α4 in the absence of UV-irradiation is likely due to masking of the XPA NLS by the binding of other cytoplasmic factors.
“likely due to the masking of the XPA NLS by the binding of other cytoplasmic factors [48], [49].”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [48]
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- Authors
- Kumar, G. R., Shum, L., & Glaunsinger, B. A.
- Affiliations
- University of California, Berkeley (US)
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2011-08
- Volume
- 31
- Issue
- 15
- Pages
- 3113-3125
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC3147611
- OpenAlex
- W2108309503
- Cited by
- 71
- References
- 79
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 2 · 2023: 4 · 2022: 7 · 2021: 6 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 1 · 2016: 3 · 2015: 8 · 2014: 6 · 2013: 4 · 2012: 10
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- W. M. Keck Foundation
- National Institutes of Health
- National Cancer Institute (R01CA136367)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- poly(A)-binding protein, importin alpha, nuclear import, RNA recognition motif, mRNA turnover, deadenylase, polyadenylated RNA, protein relocalization, gene expression regulation
- MeSH terms
- Animals, Cell Nucleus, Chlorocebus aethiops, Cytoplasm, Gene Expression Regulation, HeLa Cells, Humans, Plasmids, RNA, Messenger, Protein Biosynthesis, Viral Proteins, Herpesvirus 1, Human, COS Cells, Active Transport, Cell Nucleus, alpha Karyopherins, Poly(A)-Binding Protein I, Immunoprecipitation, HEK293 Cells
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