ArticlePloS one2016
SUMO-Modification of the La Protein Facilitates Binding to mRNA In Vitro and in Cells.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Salt-Dependent Modulation of the RNA Chaperone Activity of RNA-Binding Protein La.Methods in molecular biology (Clifton, N.J.) · 2026Article
- CPEB3 low-complexity motif regulates local protein synthesis via protein-protein interactions in neuronal ribonucleoprotein granules.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Contributive Role of Hyperglycemia and Hypoglycemia Towards the Development of Alzheimer's Disease.Molecular neurobiology · 2022Review
- Role of the RNA-binding protein La in cancer pathobiology.RNA biology · 2021Review
- La proteins couple use of sequence-specific and non-specific binding modes to engage RNA substrates.RNA biology · 2021Review
- The La-related proteins: structures and interactions of a versatile superfamily of RNA-binding proteins.RNA biology · 2021Review
- RNA-Binding Protein La Mediates TGFβ-Induced Epithelial to Mesenchymal Transition and Cancer Stem Cell Properties.Cancers · 2021Article
- SUMO Modification of the RNA-Binding Protein La Regulates Cell Proliferation and STAT3 Protein Stability.Molecular and cellular biology · 2018Article
- The La and related RNA-binding proteins (LARPs): structures, functions, and evolving perspectives.Wiley interdisciplinary reviews. RNA · 2017Review
- Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The RNA-binding protein La is involved in several aspects of RNA metabolism including the translational regulation of mRNAs and processing of pre-tRNAs. Besides its well-described phosphorylation by Casein kinase 2, the La protein is also posttranslationally modified by the Small Ubiquitin-like MOdifier (SUMO), but the functional outcome of this modification has not been defined. The objective of this study was to test whether sumoylation changes the RNA-binding activity of La. Therefore, we established an in vitro sumoylation assay for recombinant human La and analyzed its RNA-binding activity by electrophoretic mobility shift assays. We identified two novel SUMO-acceptor sites within the La protein located between the RNA recognition motif 1 and 2 and we demonstrate for the first time that sumoylation facilitates the RNA-binding of La to small RNA oligonucleotides representing the oligopyrimidine tract (TOP) elements from the 5' untranslated regions (UTR) of mRNAs encoding ribosomal protein L22 and L37 and to a longer RNA element from the 5' UTR of cyclin D1 (CCND1) mRNA in vitro. Furthermore, we show by RNA immunoprecipitation experiments that a La mutant deficient in sumoylation has impaired RNA-binding activity in cells. These data suggest that modulating the RNA-binding activity of La by sumoylation has important consequences on its functionality.
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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.