ArticleGenetics2016
BLIMP-1/BLMP-1 and Metastasis-Associated Protein Regulate Stress Resistant Development in Caenorhabditis elegans.
Article in Genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Calcium-binding protein CALU-1 is essential for proper collagen formation in Caenorhabditis elegans.Cellular and molecular life sciences : CMLS · 2025Article
- Transcriptional and spatiotemporal regulation of the dauer program.Transcription · 2023Review
- Ketamine induces apical extracellular matrix modifications in Caenorhabditis elegans.Scientific reports · 2022Article
- Specific collagens maintain the cuticle permeability barrier in Caenorhabditis elegans.Genetics · 2021Article
- Development: Keeping Time with Transcription.Current biology : CB · 2021Article
- Starvation Responses Throughout theGenetics · 2020Review
- Identifying longevity associated genes by integrating gene expression and curated annotations.PLoS computational biology · 2020Article
- Genetic interactions between the DBL-1/BMP-like pathway andMolecular biology of the cell · 2019Article
- HSP-4/BiP expression in secretory cells is regulated by a developmental program and not by the unfolded protein response.PLoS biology · 2019Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Environmental stress triggers multilevel adaptations in animal development that depend in part on epigenetic mechanisms. In response to harsh environmental conditions and pheromone signals, Caenorhabditis elegans larvae become the highly stress-resistant and long-lived dauer. Despite extensive studies of dauer formation pathways that integrate specific environmental cues and appear to depend on transcriptional reprogramming, the role of epigenetic regulation in dauer development has remained unclear. Here we report that BLMP-1, the BLIMP-1 ortholog, regulates dauer formation via epigenetic pathways; in the absence of TGF-β signaling (in daf-7 mutants), lack of blmp-1 caused lethality. Using this phenotype, we screened 283 epigenetic factors, and identified lin-40, a homolog of metastasis-associate protein 1 (MTA1) as an interactor of BLMP-1 The interaction between LIN-40 and BLMP-1 is conserved because mammalian homologs for both MTA1 and BLIMP-1 could also interact. From microarray studies, we identified several downstream target genes of blmp-1: npr-3, nhr-23, ptr-4, and sams-1 Among them S-adenosyl methionine synthase (SAMS-1), is the key enzyme for production of SAM used in histone methylation. Indeed, blmp-1 is necessary for controlling histone methylation level in daf-7 mutants, suggesting BLMP-1 regulates the expression of SAMS-1, which in turn may regulate histone methylation and dauer formation. Our results reveal a new interaction between BLMP-1/BLIMP-1 and LIN-40/MTA1, as well as potential epigenetic downstream pathways, whereby these proteins cooperate to regulate stress-specific developmental adaptations.
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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.