ArticleRNA (New York, N.Y.)2012
Both Sm-domain and C-terminal extension of Lsm1 are important for the RNA-binding activity of the Lsm1-7-Pat1 complex.
Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Global profiling of protein complex dynamics with an experimental library of protein interaction markers.Nature biotechnology · 2025Article
- Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure and function of molecular machines involved in deadenylation-dependent 5'-3' mRNA degradation.Frontiers in genetics · 2023Review
- Prognostic value and potential molecular mechanism of the like-Sm gene family in early-stage pancreatic ductal adenocarcinoma.Translational cancer research · 2021Article
- Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes.RNA (New York, N.Y.) · 2020Article
- Mutagenic Analysis of the C-Terminal Extension of Lsm1.PloS one · 2016Article
- The Lsm1-7-Pat1 complex promotes viral RNA translation and replication by differential mechanisms.RNA (New York, N.Y.) · 2015Article
- Article
- Determinants and implications of mRNA poly(A) tail size--does this protein make my tail look big?Seminars in cell & developmental biology · 2014Review
- Pat1 contributes to the RNA binding activity of the Lsm1-7-Pat1 complex.RNA (New York, N.Y.) · 2014Article
- Therapeutic modulation of eIF2α phosphorylation rescues TDP-43 toxicity in amyotrophic lateral sclerosis disease models.Nature genetics · 2014Article
- Lsm proteins and Hfq: Life at the 3' end.RNA biology · 2013Review
- Inhibition and avoidance of mRNA degradation by RNA viruses.Current opinion in microbiology · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Lsm proteins are a ubiquitous family of proteins characterized by the Sm-domain. They exist as hexa- or heptameric RNA-binding complexes and carry out RNA-related functions. The Sm-domain is thought to be sufficient for the RNA-binding activity of these proteins. The highly conserved eukaryotic Lsm1 through Lsm7 proteins are part of the cytoplasmic Lsm1-7-Pat1 complex, which is an activator of decapping in the conserved 5'-3' mRNA decay pathway. This complex also protects mRNA 3'-ends from trimming in vivo. Purified Lsm1-7-Pat1 complex is able to bind RNA in vitro and exhibits a unique binding preference for oligoadenylated RNA (over polyadenylated and unadenylated RNA). Lsm1 is a key subunit that determines the RNA-binding properties of this complex. The normal RNA-binding activity of this complex is crucial for mRNA decay and 3'-end protection in vivo and requires the intact Sm-domain of Lsm1. Here, we show that though necessary, the Sm-domain of Lsm1 is not sufficient for the normal RNA-binding ability of the Lsm1-7-Pat1 complex. Deletion of the C-terminal domain (CTD) of Lsm1 (while keeping the Sm-domain intact) impairs mRNA decay in vivo and results in Lsm1-7-Pat1 complexes that are severely impaired in RNA binding in vitro. Interestingly, the mRNA decay and 3'-end protection defects of such CTD-truncated lsm1 mutants could be suppressed in trans by overexpression of the CTD polypeptide. Thus, unlike most Sm-like proteins, Lsm1 uniquely requires both its Sm-domain and CTD for its normal RNA-binding function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.