A5077172150- Fungal and yeast genetics research
- Protein Kinase Regulation and GTPase Signaling
- DNA Repair Mechanisms
- Endoplasmic Reticulum Stress and Disease
- Fungal Biology and Applications
- Microtubule and mitosis dynamics
- Protein Tyrosine Phosphatases
- Genomics and Chromatin Dynamics
- Plant Reproductive Biology
- RNA Research and Splicing
- Genetics, Aging, and Longevity in Model Organisms
- Heat shock proteins research
- Polysaccharides and Plant Cell Walls
- Melanoma and MAPK Pathways
- Plant-Microbe Interactions and Immunity
- Nuclear Structure and Function
- Cellular Mechanics and Interactions
- Cytokine Signaling Pathways and Interactions
- Insect and Pesticide Research
- Medicinal Plant Pharmacodynamics Research
- Cancer therapeutics and mechanisms
- Synthesis and Biological Evaluation
- Carcinogens and Genotoxicity Assessment
- Plant biochemistry and biosynthesis
- PI3K/AKT/mTOR signaling in cancer
The University of Tokyo
2010-2025
MED Institute
2019
Toxicologie, Pharmacologie et Signalisation Cellulaire
2017
Tokyo University of Science
1994-2016
Apparent redundancy in two yeast osmosensors instead confers specificity coupling internal and external signals.
Abstract The yeast high osmolarity glycerol (HOG) pathway activates the Hog1 MAP kinase, which coordinates adaptation to conditions. Here we demonstrate that four-transmembrane (TM) domain protein Sho1 is an osmosensor in HKR1 sub-branch of HOG pathway. Crosslinking studies indicate forms planar oligomers dimers-of-trimers architecture by dimerizing at TM1/TM4 interface and trimerizing TM2/TM3 interface. High external induces structural changes TM domains binding cytoplasmic adaptor Ste50,...
Article3 February 2020Open Access Osmostress enhances activating phosphorylation of Hog1 MAP kinase by mono-phosphorylated Pbs2 MAP2K Kazuo Tatebayashi Corresponding Author [email protected] orcid.org/0000-0002-3131-7030 Laboratory Molecular Genetics, Frontier Research Unit, Institute Medical Science, The University Tokyo, Japan Division Cell Signaling, Department Biological Sciences, Graduate School Search for more papers this author Katsuyoshi Yamamoto Taichiro Tomida Physiology, Medicine,...
Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts characterize have been limited by their transient nature inability of current technologies distinguish direct versus bridged interactions. We report novel use cross-linking mass spectrometry (XL-MS) comprehensively Saccharomyces cerevisiae (budding yeast) protein interactome. Using this approach, we gained fundamental new insights into function, including definitive evidence self-association...
Stress-activated protein kinases (SAPKs) respond to a wide variety of stressors. In most cases, the pathways through which specific stress signals are transmitted SAPK not known. We show that yeast Hog1 is activated by acetic acid an intracellular mechanism does involve stimulation high osmolarity glycerol (HOG) signaling pathway beyond its basal level. Rather, treatment drives formation granules, function as scaffold bring together with Pbs2, immediately upstream activating kinase, in...
Hsk1, Saccharomyces cerevisiae Cdc7-related kinase in Shizosaccharomyces pombe, is required for G1/S transition and its activity controlled by the regulatory subunit Dfp1/Him1. Analyses of a newly isolated temperature-sensitive mutant, hsk1-89, reveal that Hsk1 plays crucial roles DNA replication checkpoint signaling maintenance proper chromatin structures during mitotic S phase through regulating functions Rad3 (ATM)-Cds1 Rad21 (cohesin), respectively, addition to expected essential...
Background Bloom's syndrome (BS) is an autosomal recessive disorder causing short stature, immunodeficiency, and increased risk of cancer. Increased rates sister chromatid exchange chromosomal aberration have been observed in cells having defects the BLM gene. Among five kinds human RecQ helicases cloned, mutations WRN RecQL4 known as causes premature ageing. Little is, however, about function helicase Results We show that , but not can prevent ageing homologous recombination at rDNA loci...
In Saccharomyces cerevisiae, external high osmolarity activates the Hog1 mitogen-activated protein kinase (MAPK), which controls various aspects of osmoadaptation. Ssk1 is a homolog bacterial two-component response regulators and Ssk2 MAPK upstream Hog1. It has been proposed that unphosphorylated (Ssk1-OH) active form phosphorylated (Ssk1 approximately P) at Asp554 by Sln1-Ypd1-Ssk1 multistep phosphorelay mechanism inactive form. this study, we show constitutive activation occurs when...
Abstract The fission yeast DNA repair gene rad21+ is essential for cell growth. To investigate the function proliferation, we have isolated a temperature-sensitive mutant of gene. mutant, rad21-K1, showed abnormal mitosis at nonpermissive temperature. Some cells contained nuclear structures, such as condensed chromosomes with short spindles, or stretched unequally separated by elongating spindles. Other exhibited displaced nucleus cut-like phenotype. Similar abnormalities were observed when...
Functional interactions between a mitogen-activated protein kinase (MAPK) and its regulators require specific docking interactions.Here, we investigated the mechanism by which yeast osmoregulatory Hog1 MAPK specifically interacts with activator, Pbs2, major inactivator, phosphatase Ptp2.We found, in N-terminal noncatalytic region of Hog1-binding domain, termed HBD-1.We also defined two adjacent Pbs2-binding sites Hog1, namely, common (CD) domain 2 (PBD-2).The PBD-2 site appears to be...
In the budding yeast Saccharomyces cerevisiae, osmostress activates Hog1 mitogen-activated protein kinase (MAPK), which regulates diverse osmoadaptive responses. Hkr1 is a large, highly glycosylated, single-path transmembrane that putative osmosensor in one of upstream pathways termed HKR1 subbranch. The extracellular region contains both positive and negative regulatory domain. However, function cytoplasmic domain (Hkr1-cyto) unknown. Here, using mass spectrometric method, we identified...
To adapt to environmental high osmolarity, the budding yeast Saccharomyces cerevisiae activates Hog1 mitogen-activated protein kinase, which regulates diverse osmoadaptive responses. is activated through high-osmolarity glycerol (HOG) pathway, consists of independent upstream signaling routes termed SLN1 branch and SHO1 branch. Here, we report that extracellular cysteine-rich (CR) domain transmembrane-anchor Opy2 binds Hkr1-Msb2 homology (HMH) putative osmosensor Msb2 formation Opy2-Msb2...
To cope with an increased external osmolarity, the budding yeast Saccharomyces cerevisiae activates Hog1 mitogen-activated protein kinase (MAPK) through high-osmolarity glycerol (HOG) pathway, which governs adaptive responses to osmostress. In HOG two apparently redundant upstream branches, termed SLN1 and SHO1, activate cognate MAP3Ks (MAPKK kinase) Ssk2/22 Ste11, respectively. These MAP3Ks, when activated, phosphorylate thus Pbs2 MAP2K (MAPK kinase), in turn phosphorylates Hog1. Previous...
To cope with increased extracellular osmolarity, the budding yeast Saccharomyces cerevisiae activates Hog1 mitogen-activated protein kinase (MAPK), which controls a variety of adaptive responses. is activated through high-osmolarity glycerol (HOG) pathway, consists core MAPK cascade and two independent upstream branches (SHO1 SLN1 branches) containing distinct osmosensing machineries. In SHO1 branch, homo-oligomer Sho1, four-transmembrane (TM) osmosensor, interacts transmembrane...