ArticlePloS one2014
Role of LARP6 and nonmuscle myosin in partitioning of collagen mRNAs to the ER membrane.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- RNA-binding protein LARP6 coordinates hepatic stellate cell activation and liver fibrosis.The Journal of clinical investigation · 2026Article
- The LARP6 La module fromRNA biology · 2025Article
- Regulation of Hepatic Stellate Cell Phenotypes in Metabolic Dysfunction-Associated Steatohepatitis.Gastroenterology · 2025Review
- Cardiomyocyte-specific LARP6 overexpression prevents angiotensin II-induced myocardial dysfunction and interstitial fibrosis.American journal of physiology. Heart and circulatory physiology · 2025Article
- Noncanonical RNA binding of human La-related protein 6.Nucleic acids research · 2025Article
- Article
- A Robust Expression and Purification Protocol for the Production of the La Domain of Human LARP6.ACS omega · 2025Article
- eIF4E1b is a non-canonical eIF4E protecting maternal dormant mRNAs.EMBO reports · 2024Article
- Characterization of Sequence-Specific Binding of LARP6 to the 5' Stem-Loop of Type I Collagen mRNAs and Implications for Rational Design of Antifibrotic Drugs.Journal of molecular biology · 2022Article
- Imaging of type I procollagen biosynthesis in cells reveals biogenesis in highly organized bodies; Collagenosomes.Matrix biology plus · 2021Article
- Discovery of a Lead Compound for Specific Inhibition of Type I Collagen Production in Fibrosis.ACS medicinal chemistry letters · 2021Article
- Maternal Larp6 controls oocyte development, chorion formation and elevation.Development (Cambridge, England) · 2020Article
- Heterogeneous translational landscape of the endoplasmic reticulum revealed by ribosome proximity labeling and transcriptome analysis.The Journal of biological chemistry · 2019Article
- Discovery and evaluation of inhibitor of LARP6 as specific antifibrotic compound.Scientific reports · 2019Article
- mTORC1 phosphorylates LARP6 to stimulate type I collagen expression.Scientific reports · 2017Article
- LARP6 Meets Collagen mRNA: Specific Regulation of Type I Collagen Expression.International journal of molecular sciences · 2016Review
- Akt mediated phosphorylation of LARP6; critical step in biosynthesis of type I collagen.Scientific reports · 2016Article
- The La-Related Proteins, a Family with Connections to Cancer.Biomolecules · 2015Review
- LARP4B is an AU-rich sequence associated factor that promotes mRNA accumulation and translation.RNA (New York, N.Y.) · 2015Article
- Diversity and selectivity in mRNA translation on the endoplasmic reticulum.Nature reviews. Molecular cell biology · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Type I collagen is extracellular matrix protein composed of two α1(I) and one α2(I) polypeptides that fold into triple helix. Collagen polypeptides are translated in coordination to synchronize the rate of triple helix folding to the rate of posttranslational modifications of individual polypeptides. This is especially important in conditions of high collagen production, like fibrosis. It has been assumed that collagen mRNAs are targeted to the membrane of the endoplasmic reticulum (ER) after translation of the signal peptide and by signal peptide recognition particle (SRP). Here we show that collagen mRNAs associate with the ER membrane even when translation is inhibited. Knock down of LARP6, an RNA binding protein which binds 5' stem-loop of collagen mRNAs, releases a small amount of collagen mRNAs from the membrane. Depolimerization of nonmuscle myosin filaments has a similar, but stronger effect. In the absence of LARP6 or nonmuscle myosin filaments collagen polypeptides become hypermodified, are poorly secreted and accumulate in the cytosol. This indicates lack of coordination of their synthesis and retro-translocation due to hypermodifications and misfolding. Depolimerization of nonmuscle myosin does not alter the secretory pathway through ER and Golgi, suggesting that the role of nonmuscle myosin is primarily to partition collagen mRNAs to the ER membrane. We postulate that collagen mRNAs directly partition to the ER membrane prior to synthesis of the signal peptide and that LARP6 and nonmuscle myosin filaments mediate this process. This allows coordinated initiation of translation on the membrane bound collagen α1(I) and α2(I) mRNAs, a necessary step for proper synthesis of type I collagen.
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Registered trials
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