ArticleThe EMBO journal1996
A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 182 citations in OpenAlex.
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
- Association analysis of HSP90AA1 polymorphism with thermotolerance in tropically adapted Indian crossbred cattle.Tropical animal health and production · 2024Article
- Loss of Grp170 results in catastrophic disruption of endoplasmic reticulum function.Molecular biology of the cell · 2024Article
- Genome-wide screen identifies new set of genes for improved heterologous laccase expression in Saccharomyces cerevisiae.Microbial cell factories · 2024Article
- Dosage suppressors of gpn2ts mutants and functional insights into the role of Gpn2 in budding yeast.PloS one · 2024Article
- Lhs1 dependent ERAD is determined by transmembrane domain context.The Biochemical journal · 2023Article
- Multifarious Translational Regulation during Replicative Aging in Yeast.Journal of fungi (Basel, Switzerland) · 2022Article
- Key infection stages defending heat stress in high-temperature-resistantFrontiers in microbiology · 2022Article
- Role of the HSP70 Co-Chaperone SIL1 in Health and Disease.International journal of molecular sciences · 2021Review
- The Role of Endoplasmic Reticulum Chaperones in Protein Folding and Quality Control.Progress in molecular and subcellular biology · 2021Article
- Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit.Open biology · 2020Article
- Identification of differentially expressed microRNAs in Sahiwal (Bos indicus) breed of cattle during thermal stress.Cell stress & chaperones · 2018Article
- Genetic polymorphism in Hsp90AA1 gene is associated with the thermotolerance in Chinese Holstein cows.Cell stress & chaperones · 2018Article
- Differential expression of microRNAs associated with thermal stress in Frieswal (Bos taurus x Bos indicus) crossbred dairy cattle.Cell stress & chaperones · 2018Article
- Characterization of aromatic residue-controlled protein retention in the endoplasmic reticulum ofThe Journal of biological chemistry · 2017Article
- Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein.The Biochemical journal · 2017Article
- Protein aggregation activates erratic stress response in dietary restricted yeast cells.Scientific reports · 2016Article
- Crosstalk between cellular compartments protects against proteotoxicity and extends lifespan.Scientific reports · 2016Article
- Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.Molecular & cellular proteomics : MCP · 2016Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast genome sequencing project predicts an open reading frame (YKL073) that would encode a novel member of the Hsp70 family of molecular chaperones. We report that this 881 codon reading frame represents a functional gene expressing a 113-119 kDa glycoprotein localized within the lumen of the endoplasmic reticulum (ER). We therefore propose to designate this gene LHS1 (Lumenal Hsp Seventy). Our studies indicate that LHS1 is regulated by the unfolded protein response pathway, as evidenced by its transcriptional induction in cells treated with tunicamycin, and in various mutants defective in precursor processing (sec11-7, sec53-6 and sec59-1). LHS1 is not essential for viability, but an Lhs1 null mutant strain exhibits a coordinated induction of genes regulated by the unfolded protein response indicating a role for Lhs1p in protein folding in the ER. Furthermore, the null mutation is synthetically lethal in combination with (delta)ire1, thus activation of the unfolded protein response pathway is essential for cells to tolerate loss of Lhs1p. Synthetically lethality is also seen with mutations in KAR2, strongly suggesting that Kar2p and Lhs1p have overlapping functions. The Lhs1 null mutant exhibits a severe constitutive defect in the translocation of several secretory preproteins. We therefore propose that Lhs1p is a molecular chaperone of the ER lumen involved in both polypeptide translocation and subsequent protein folding.
Indexed as
Identifiers
8654361PMC450199W195389358What OpenQuestion holds
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.