ArticleThe EMBO journal2000
LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 188 citations in OpenAlex.
- Hac1-independent functions of Ire1 drive morphogenesis in Candida albicans through distinct transcriptional programs.Journal of cell science · 2026Article
- Transcriptomics analysis identifies folding and secretion related genes for improving monoclonal antibody production in Thermothelomyces heterothallica C1.Microbial cell factories · 2026Article
- Review
- The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis.Journal of molecular biology · 2024Review
- Loss of Grp170 results in catastrophic disruption of endoplasmic reticulum function.Molecular biology of the cell · 2024Article
- The genetic basis of hydrocephalus: genes, pathways, mechanisms, and global impact.Fluids and barriers of the CNS · 2024Review
- EngineeringEngineering microbiology · 2024Review
- Genome-wide screen identifies new set of genes for improved heterologous laccase expression in Saccharomyces cerevisiae.Microbial cell factories · 2024Article
- Up Front Unfolded Protein Response Combined with Early Protein Secretion Pathway Engineering inInternational journal of molecular sciences · 2023Article
- Lhs1 dependent ERAD is determined by transmembrane domain context.The Biochemical journal · 2023Article
- Diverse Sphingolipid Species Harbor Different Effects on Ire1 Clustering.International journal of molecular sciences · 2022Article
- The molecular chaperone GRP170 protects against ER stress and acute kidney injury in mice.JCI insight · 2022Article
- The regulatory role of endoplasmic reticulum chaperone proteins in neurodevelopment.Frontiers in neuroscience · 2022Review
- Reprogramming of the Ethanol Stress Response in Saccharomyces cerevisiae by the Transcription Factor Znf1 and Its Effect on the Biosynthesis of Glycerol and Ethanol.Applied and environmental microbiology · 2021Article
- Combined Transcriptomic and Proteomic Analysis of Perk Toxicity Pathways.International journal of molecular sciences · 2021Article
- Role of the HSP70 Co-Chaperone SIL1 in Health and Disease.International journal of molecular sciences · 2021Review
- The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.The Journal of biological chemistry · 2020Article
- The endoplasmic reticulum chaperone PfGRP170 is essential for asexual development and is linked to stress response in malaria parasites.Cellular microbiology · 2019Article
- Protein Quality Control in the Endoplasmic Reticulum.The protein journal · 2019Review
- Functional Role of SIL1 in Neurodevelopment and Learning.Neural plasticity · 2019Article
16 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Lhs1p is an Hsp70-related chaperone localized in the endoplasmic reticulum (ER) lumen. Deltalhs1 mutant cells are viable but are constitutively induced for the unfolded protein response (UPR). Here, we demonstrate a severe growth defect in Deltaire1Deltalhs1 double mutant cells in which the UPR can no longer be induced. In addition, we have identified a UPR- regulated gene, SIL1, whose overexpression is sufficient to suppress the Deltaire1Deltalhs1 growth defect. SIL1 encodes an ER-localized protein that interacts directly with the ATPase domain of Kar2p (BiP), suggesting some role in modulating the activity of this vital chaperone. SIL1 is a non-essential gene but the Deltalhs1Deltasil1 double mutation is lethal and correlates with a complete block of protein translocation into the ER. We conclude that the IRE1-dependent induction of SIL1 is a vital adaptation in Deltalhs1 cells, and that the activities associated with the Lhs1 and Sil1 proteins constitute an essential function required for protein translocation into the ER. The Sil1 protein appears widespread amongst eukaryotes, with homologues in Yarrowia lipolytica (Sls1p), Drosophila and mammals.
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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.