Human Pumilio Proteins Recruit Multiple Deadenylases to Efficiently Repress Messenger RNAs
Open accessAbstract
PUF proteins are a conserved family of eukaryotic RNA-binding proteins that regulate specific mRNAs: they control many processes including stem cell proliferation, fertility, and memory formation. PUFs repress protein expression from their target mRNAs but the mechanism by which they do so remains unclear, especially for humans. Humans possess two PUF proteins, PUM1 and PUM2, which exhibit similar RNA binding specificities. Here we report new insights into their regulatory activities and mechanisms of action. We developed functional assays to measure sequence-specific repression by PUM1 and PUM2. Both robustly inhibit translation and promote mRNA degradation. Purified PUM complexes were found to contain subunits of the CCR4-NOT (CNOT) complex, which contains multiple enzymes that catalyze mRNA deadenylation. PUMs interact with the CNOT deadenylase subunits in vitro. We used three approaches to determine the importance of deadenylases for PUM repression. First, dominant-negative mutants of CNOT7 and CNOT8 reduced PUM repression. Second, RNA interference depletion of the deadenylases alleviated PUM repression. Third, the poly(A) tail was necessary for maximal PUM repression. These findings demonstrate a conserved mechanism of PUF-mediated repression via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. A second, deadenylation independent mechanism was revealed by the finding that PUMs repress an mRNA that lacks a poly(A) tail. Thus, human PUMs are repressors capable of deadenylation-dependent and -independent modes of repression.
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For PUM1 and PUM2, the predicted direction of effect was counter to expectation, indicating that correlation may reflect possible additional functional roles for these proteins and/or their binding motifs.
“In other cases (for example, PUM1 and PUM2), the direction of the effect was counter to expectation33, indicating that correlation may reflect possible additional functional roles for these proteins and/or their binding motifs.”
From A compendium of RNA-binding motifs for decoding gene regulation (2013) · cites this paper as [33]
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- Authors
- Van Etten, J., Schagat, T. L., Hrit, J., Weidmann, C. A., Brumbaugh, J., Coon, J. J., & Goldstrohm, A. C.
- Affiliations
- Promega (United States) (US)
- University of Michigan (US)
- University of Wisconsin–Madison (US)
- Corresponding author
- Goldstrohm, Aaron C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-10
- Volume
- 287
- Issue
- 43
- Pages
- 36370-36383
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3476303
- OpenAlex
- W2153368605
- Cited by
- 205
- References
- 89
- Citations by year
- 2026: 10 · 2025: 9 · 2024: 17 · 2023: 15 · 2022: 8 · 2021: 15 · 2020: 16 · 2019: 25 · 2018: 21 · 2017: 17 · 2016: 12 · 2015: 12 · 2014: 17 · 2013: 11
- FWCI
- 5.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM007544)
- 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
- PUM1, PUM2, PUF proteins, mRNA deadenylation, CCR4-NOT complex, CNOT7, poly(A) tail, protein synthesis inhibition, mRNA degradation, RNA-binding proteins
- MeSH terms
- Biological Assay, Exoribonucleases, Humans, Multienzyme Complexes, Poly A, Repressor Proteins, RNA, Messenger, Transcription Factors, Protein Biosynthesis, RNA-Binding Proteins, Protein Structure, Tertiary, RNA Stability, HEK293 Cells
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