Masaaki Tatsuka

ORCID: 0000-0002-9806-7398
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About
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Research Areas
  • Microtubule and mitosis dynamics
  • Cancer-related Molecular Pathways
  • Cell death mechanisms and regulation
  • Protein Kinase Regulation and GTPase Signaling
  • Plant nutrient uptake and metabolism
  • DNA Repair Mechanisms
  • RNA Interference and Gene Delivery
  • Viral Infectious Diseases and Gene Expression in Insects
  • Cancer Research and Treatments
  • CRISPR and Genetic Engineering
  • Ubiquitin and proteasome pathways
  • Molecular Biology Techniques and Applications
  • Genomics and Chromatin Dynamics
  • Cellular transport and secretion
  • Photosynthetic Processes and Mechanisms
  • RNA modifications and cancer
  • Cancer Cells and Metastasis
  • Cancer, Hypoxia, and Metabolism
  • HER2/EGFR in Cancer Research
  • Peptidase Inhibition and Analysis
  • Cellular Mechanics and Interactions
  • Cell Adhesion Molecules Research
  • Epigenetics and DNA Methylation
  • Mechanisms of cancer metastasis
  • Radiation Effects and Dosimetry

Prefectural University of Hiroshima
2011-2021

University Hospital Carl Gustav Carus
2010

Heinrich Heine University Düsseldorf
2010

University Medical Center Hamburg-Eppendorf
2010

Universität Hamburg
2010

Leipzig University
2010

University of Bonn
2010

University Hospital of Zurich
2010

Hiroshima University
1999-2008

Kanazawa Medical University
1996-2004

The function of Aurora-C kinase, a member the Aurora kinase family identified in mammals, is currently unknown. We present evidence that Aurora-C, like Aurora-B chromosomal passenger protein localizing first to centromeres and then midzone mitotic cells. transcript expressed at moderate level albeit about an order magnitude lower than diploid human fibroblasts. elevated several cancer cell types. mRNA expressions are maximally during G2/M phase but their expression profiles synchronized...

10.1002/cm.20039 article EN Cell Motility and the Cytoskeleton 2004-10-21

Mitotic kinases regulate cell division and its checkpoints, errors of which can lead to aneuploidy or genetic instability. One these is Aurora-B, a key kinase that required for chromosome alignment at the metaphase plate cytokinesis in mammalian cells. We report here human Aurora-B phosphorylated Thr-232 through interaction with inner centromere protein (INCENP) vivo. The phosphorylation occurs by means an autophosphorylation mechanism, indispensable activity. activation spatio-temporally...

10.1074/jbc.m311128200 article EN cc-by Journal of Biological Chemistry 2004-03-01

Aurora-B is an evolutionally conserved protein kinase that regulates several mitotic events including cytokinesis. We previously demonstrated the possible existence of a phosphorylates at least Ser-72 on vimentin, most widely expressed intermediate filament protein, in cleavage furrow-specific manner. Here we showed vimentin-Ser-72 phosphorylation occurred specifically border Aurora-B-localized area from anaphase to telophase. Expression dominant-negative mutant led reduction this...

10.1074/jbc.m210892200 article EN cc-by Journal of Biological Chemistry 2003-02-28

Aurora B is a protein kinase and chromosomal passenger that undergoes dynamic redistribution during mitosis. We have probed the mechanism regulates its localization with cells expressing green fluorescent (GFP)-tagged wild-type or mutant aurora B. was found at centromeres prophase persisted until ∼0.5 min after anaphase onset, when it redistributed to spindle midzone became concentrated equator along microtubules. Depolymerization of microtubules inhibited dissociation from early caused...

10.1091/mbc.01-09-0467 article EN Molecular Biology of the Cell 2002-04-01

Nonessential tRNA modifications by methyltransferases are evolutionarily conserved and have been reported to stabilize mature molecules prevent rapid decay (RTD). The modifying enzymes, NSUN2 METTL1, mammalian orthologs of yeast Trm4 Trm8, which required for protecting against RTD. A simultaneous overexpression METTL1 is widely observed among human cancers suggesting that targeting both proteins provides a novel powerful strategy cancer chemotherapy. Here, we show combined knockdown in HeLa...

10.1371/journal.pgen.1004639 article EN cc-by PLoS Genetics 2014-09-18

STK15 is an Aurora/Ipl-1 related serine/threonine kinase that associated with centrosomes and induces aneuploidy when overexpressed in mammalian cells. It well known phosphorylation dephosphorylation of kinases are important for regulation their activity. But mechanisms by which activity regulated have not been elucidated. We report contains two functional binding sites protein phosphatase type 1 (PP1), the these proteins cell cycle-regulated peaking at mitosis. Activated mitosis...

10.1074/jbc.m107540200 article EN cc-by Journal of Biological Chemistry 2001-12-01

NSUN2, also known as SAKI or MISU, is a methyltransferase which catalyses (cytosine-5-)-methylation of tRNA. The human NSUN2 gene located on chromosome 5p15.31-33. We show that copy number increased in oral and colorectal cancers. Protein expression levels were determined by immunoblot using novel polyclonal antibodies raised against synthetic peptide corresponding to the C-terminal region protein. In most normal tissues, extremely low. On other hand, cancers typically expressed high NSUN2....

10.1089/dna.2011.1446 article EN DNA and Cell Biology 2011-12-03

Aurora-B is a protein kinase required for chromosome segregation and the progression of cytokinesis during cell cycle. We report here that phosphorylates GFAP desmin in vitro, this phosphorylation leads to reduction filament forming ability. The sites phosphorylated by Aurora-B; Thr-7/Ser-13/Ser-38 GFAP, Thr-16 are common with those related Rho-associated (Rho-kinase), which has been reported phosphorylate at cleavage furrow cytokinesis. identified Ser-59 be specific site vitro. Use an...

10.1091/mbc.e02-09-0612 article EN Molecular Biology of the Cell 2003-04-01

Disassembly of the nucleolus during mitosis is driven by phosphorylation nucleolar proteins. RNA processing stops until completion reformation in G(1) phase. Here, we describe methyltransferase NSUN2, a novel substrate Aurora-B that contains an NOL1/NOP2/sun domain. NSUN2 was concentrated interphase and distributed perichromosome cytoplasm mitosis. phosphorylated at Ser139. Nucleolar proteins NPM1/nucleophosmin/B23 nucleolin/C23 were associated with interphase. In mitotic cells, association...

10.1091/mbc.e06-11-1021 article EN Molecular Biology of the Cell 2007-01-11

Poly(ADP-ribose) polymerase (PARP) is an enzyme that mediates post-translational modification of proteins. Seventeen known members the PARP superfamily can be grouped into three classes based on catalytic activity: (i) classical poly(ADP-ribose) polymerases, (ii) mono(ADP‑ribosyl) transferases and (iii) catalytically inactive members. PARP6 belongs to mono(ADP-ribosyl) transferase class, here we have found a negative regulator cell proliferation. Forced expression in HeLa cells induced...

10.3892/ijo.2012.1652 article EN International Journal of Oncology 2012-01-01

Survivin, a member of the inhibitor apoptosis protein family, has attracted growing attention due to its expression in various tumors and potential application tumor therapy. However, subcellular localization function have remained controversial: Recent studies revealed that survivin is localized at mitotic spindle, binds caspases, could thus protect cells from apoptosis. The cell cycle-dependent antiapoptotic led hypothesis connects cycle with apoptosis, providing death switch for...

10.1091/mbc.e02-04-0182 article EN Molecular Biology of the Cell 2003-01-01

Journal Article Myosin II Regulatory Light Chain as a Novel Substrate for AIM-1, an Aurora/Ipl1p-related Kinase from Rat Get access Maki Murata-Hori, Murata-Hori *Department of Biological Science, Graduate School Hiroshima UniversityHigashi-Hiroshima 739-8526 Search other works by this author on: Oxford Academic PubMed Google Scholar Katsumi Fumoto, Fumoto Yasuaki Fukuta, Fukuta Takahiro Iwasaki, Iwasaki Asako Kikuchi, Kikuchi Masaaki Tatsuka, Tatsuka †Department Radiobiology, Research...

10.1093/oxfordjournals.jbchem.a022840 article EN The Journal of Biochemistry 2000-12-01
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