ArticleMolecular and cellular biology1997
FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 38 citations in OpenAlex.
- FK506-binding protein, FKBP12, promotes serine utilization and negatively regulates threonine deaminase in fission yeast.iScience · 2022Article
- Fpr1, a primary target of rapamycin, functions as a transcription factor for ribosomal protein genes cooperatively with Hmo1 in Saccharomyces cerevisiae.PLoS genetics · 2020Article
- Production of (S)-2-aminobutyric acid and (S)-2-aminobutanol in Saccharomyces cerevisiae.Microbial cell factories · 2017Article
- Article
- Accumulation of a threonine biosynthetic intermediate attenuates general amino acid control by accelerating degradation of Gcn4 via Pho85 and Cdk8.PLoS genetics · 2014Article
- Multiplex assay for condition-dependent changes in protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Homoserine toxicity in Saccharomyces cerevisiae and Candida albicans homoserine kinase (thr1Delta) mutants.Eukaryotic cell · 2010Article
- Rapamycin inhibits yeast nucleotide excision repair independently of tor kinases.Toxicological sciences : an official journal of the Society of Toxicology · 2010Article
- Podospora anserina target of rapamycin.Current genetics · 2006Article
- Regulation of leucine uptake by tor1+ in Schizosaccharomyces pombe is sensitive to rapamycin.Genetics · 2005Article
- FKBP12 controls aspartate pathway flux in Saccharomyces cerevisiae to prevent toxic intermediate accumulation.Eukaryotic cell · 2004Article
- Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine dehydrogenase gene isolated by functional complementation of a yeast hom6 mutant.Plant molecular biology · 2003Article
- Gene activation by interaction of an inhibitor with a cytoplasmic signaling protein.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Metal-dependent nucleotide binding to the Escherichia coli rotamase SlyD.The Biochemical journal · 1999Article
- Rapamycin antifungal action is mediated via conserved complexes with FKBP12 and TOR kinase homologs in Cryptococcus neoformans.Molecular and cellular biology · 1999Article
- Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.Genetics · 1999Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The peptidyl-prolyl isomerase FKBP12 was originally identified as the intracellular receptor for the immunosuppressive drugs FK506 (tacrolimus) and rapamycin (sirolimus). Although peptidyl-prolyl isomerases have been implicated in catalyzing protein folding, the cellular functions of FKBP12 in Saccharomyces cerevisiae and other organisms are largely unknown. Using the yeast two-hybrid system, we identified aspartokinase, an enzyme that catalyzes an intermediate step in threonine and methionine biosynthesis, as an in vivo binding target of FKBP12. Aspartokinase also binds FKBP12 in vitro, and drugs that bind the FKBP12 active site, or mutations in FKBP12 surface and active site residues, disrupt the FKBP12-aspartokinase complex in vivo and in vitro.fpr1 mutants lacking FKBP12 are viable, are not threonine or methionine auxotrophs, and express wild-type levels of aspartokinase protein and activity; thus, FKBP12 is not essential for aspartokinase activity. The activity of aspartokinase is regulated by feedback inhibition by product, and genetic analyses reveal that FKBP12 is important for this feedback inhibition, possibly by catalyzing aspartokinase conformational changes in response to product binding.
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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.