{"id":28,"date":"2026-05-18T13:30:29","date_gmt":"2026-05-18T04:30:29","guid":{"rendered":"https:\/\/www-p.sci.ocha.ac.jp\/hiranolab-test\/?page_id=28"},"modified":"2026-05-19T16:19:19","modified_gmt":"2026-05-19T07:19:19","slug":"publications","status":"publish","type":"page","link":"https:\/\/www-p.sci.ocha.ac.jp\/hiranolab\/publications\/","title":{"rendered":"\u7814\u7a76\u696d\u7e3e(Publications)"},"content":{"rendered":"\n<h2 class=\"wp-block-heading\">\u539f\u8457\u8ad6\u6587(Original articles)<\/h2>\n\n\n\n<h3 class=\"wp-block-heading\">2021\u5e74-<\/h3>\n\n\n\n<ul class=\"wp-block-list\">\n<li>[preprint] Sakai Y<sup>#<\/sup>, Ariyoshi M<sup>#<\/sup>, Hirano Y<sup>#<\/sup> (<sup>#<\/sup>\u5171\u540c\u7b2c\u4e00\u8457\u8005), Suzuki A, Hirota T, Tachikawa M, Fukagawa T. \u201cCCAN forms the spherical shell-like structure in interphase kinetochores\u201d bioRxiv, DOI: 10.64898\/2026.01.14.699427 (2026)<\/li>\n\n\n\n<li>Kong W, Hara M, Tokunaga Y, Okumura K, Hirano Y, Miao J, Takenoshita Y, Hashimoto M, Sasaki H, Fujimori T, Wakabayashi Y, Fukagawa T. \u201cCENP-C-Mis12 complex establishes a regulatory loop through Aurora B for chromosome segregation\u201d <em>Life Sci. Alliance<\/em>, <strong>8(1)<\/strong>: e202402927 (2024) DOI: 10.26508\/lsa.202402927<\/li>\n\n\n\n<li>Hirano Y(*\u8cac\u4efb\u8457\u8005), Sato T, Miura A, Kubota Y, Shindo K, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. \u201cDisordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity\u201d <em>J. Biol. Chem, <\/em><strong>300(7)<\/strong>: 107430 (2024) DOI: 10.1016\/j.jbc.2024.107430<\/li>\n\n\n\n<li>Nagpal H, Ali-Ahmad A, Hirano Y, Cai W, Halic M, Fukagawa T, Sekulic N, Firez B. \u201cCENP-A and CENP-B collaborate to create an open centromeric chromatin state\u201d <em>Nat. Commun.<\/em>, <strong>14(1)<\/strong>: 8227 (2023) DOI: 10.1038\/s41467-023-43739-5<\/li>\n\n\n\n<li>Le TK, Hirano Y, Asakawa H, Okamoto K, Fukagawa T, Haraguchi T, Hiraoka Y. \u201cA ubiquitin\u2013proteasome pathway degrades the inner nuclear membrane protein Bqt4 to maintain nuclear membrane homeostasis\u201d <em>J. Cell Sci.<\/em>, <strong>136(19)<\/strong>: jcs260930 (2023) DOI: 10.1242\/jcs.260930<\/li>\n\n\n\n<li>Hirano Y(*\u8cac\u4efb\u8457\u8005), Kinugasa Y, Kubota Y, Obuse C, Haraguchi T, Hiraoka Y*. \u201cInner nuclear membrane proteins Lem2 and Bqt4 interact with different lipid synthesis enzymes in fission yeast\u201d <em>J. Biochem.<\/em>, <strong>174(1)<\/strong>: 33\u201346 (2023) DOI: 10.1093\/jb\/mvad017<br><mark style=\"background-color:rgba(0, 0, 0, 0);color:#d70000\" class=\"has-inline-color\">Journal cover, \u7b2c32\u56deJB\u8ad6\u6587\u8cde\u306b\u9078\u51fa<\/mark><\/li>\n\n\n\n<li>Hirano Y(*\u8cac\u4efb\u8457\u8005), Ohno Y, Kubota Y, Fukagawa T, Kihara A, Haraguchi T, Hiraoka Y*. \u201cCeramide synthase homolog Tlc4 maintains nuclear envelope integrity via its Golgi translocation\u201d <em>J. Cell Sci.<\/em>, <strong>136(10)<\/strong>: jcs260923 (2023) DOI: 10.1242\/jcs.260923<br><mark style=\"background-color:rgba(0, 0, 0, 0);color:#c00000\" class=\"has-inline-color\">First person\u3068\u3057\u3066\u7d39\u4ecb\u3055\u308c\u305f<\/mark><\/li>\n\n\n\n<li>Watabe M, Hirano Y, Iwane A, Matoba O, Takahashi K. \u201cOptical dispersions through intracellular inhomogeneities\u201d <em>Phys. Rev. Res.<\/em>, <strong>5(2)<\/strong>: L022043 (2023) DOI: 10.1103\/PhysRevResearch.5.L022043<\/li>\n\n\n\n<li>Asakawa H, Hirano Y, Shindo T, Haraguchi T, Hiraoka Y. \u201cFission yeast Ish1 and Les1 interact with each other in the lumen of the nuclear envelope\u201d <em>Genes Cells<\/em>, <strong>27(11)<\/strong>: 643-656 (2022) DOI: 10.1111\/gtc.12981<\/li>\n\n\n\n<li>Hiraoka H, Wang J, Nakano T, Hirano Y, Yamazaki S, Hiraoka Y, Haraguchi T. \u201cATP levels influence cell movement during the mound phase in Dictyostelium discoideum as revealed by ATP visualization and simulation\u201d <em>FEBS Open Bio.<\/em>, <strong>12(11)<\/strong>: 2042-2056 (2022) DOI: 10.1002\/2211-5463.13480<\/li>\n\n\n\n<li>Martin Caballero L, Capella M, Barrales RR, Dobrev N, van Emden T, Hirano Y, Suma Sreechakram VN, Fischer-Burkart S, Kinugasa Y, Nevers A, Rougemaile M, Sinnig I, Fischer T, Hiraoka Y, Braun S. \u201cThe inner nuclear membrane protein Lem2 coordinates RNA degradation at the nuclear periphery\u201d <em>Nat. Struct. Mol. Biol.<\/em>,<strong> 29<\/strong>, 910-921 (2022) DOI: 10.1038\/s41594-022-00831-6<\/li>\n\n\n\n<li>Watanabe R, Hirano Y, Hara M, Hiraoka Y, Fukagawa T. &#8220;Mobility of kinetochore proteins measured by FRAP analysis in living cells&#8221; <em>Chromosome Res.<\/em>, <strong>30(1)<\/strong>: 43-57 (2022) DOI: 10.1007\/s10577-021-09678-x<\/li>\n\n\n\n<li>Haraguchi T, Koujin T, Shindo T, Bilir S, Osakada H, Nishimura K, Hirano Y, Asakawa H, Mori C, Kobayashi S, Okada Y, Chikashige Y, Fukagawa T, Shibata S, Hiraoka Y. \u201cTransfected plasmid DNA is incorporated into the nucleus via nuclear envelope reformation at telophase\u201d <em>Commun. Biol.<\/em>, <strong>5(1)<\/strong>:78 (2022) DOI: 10.1038\/s42003-022-03021-8<\/li>\n\n\n\n<li>Hayashi-Takanaka Y, Hayashi Y, Hirano Y, Miyawaki-Kuwakado A, Ohkawa Y, Obuse C, Kimura H, Haraguchi T, Hiraoka Y. &#8220;Chromatin loading of MCM hexamers is associated with di-\/tri-methylation of histone H4K20 toward S phase entry&#8221; <em>Nucleic Acids Res.<\/em>, <strong>49(21)<\/strong>: 12152-12166 (2021) DOI: 10.1093\/nar\/gkab1068<\/li>\n<\/ul>\n\n\n\n<h3 class=\"wp-block-heading\">2003-2020\u5e74<\/h3>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Hirano Y(*\u8cac\u4efb\u8457\u8005), Kinugasa Y, Osakada H, Shindo T, Kubota Y, Shibata S, Haraguchi T, Hiraoka Y*. &#8220;Lem2 and Lnp1 maintain the membrane boundary between the nuclear envelope and endoplasmic reticulum&#8221; <em>Commun. Biol.<\/em>, <strong>3(1)<\/strong>:276 (2020) DOI : 10.1038\/s42003-020-0999-9<\/li>\n\n\n\n<li>Hiraoka H, Nakano T, Kuwana S, Fukuzawa M, Hirano Y, Ueda M, Haraguchi T, Hiraoka Y. &#8220;Intracellular ATP levels influence cell fates in Dictyostelium discoideum differentiation&#8221; <em>Genes Cells<\/em>, <strong>25(5)<\/strong>: 312-32 (2020) DOI: 10.1111\/gtc.12763<\/li>\n\n\n\n<li>Osemwenkhae OP, Sakuno T, Hirano Y, Asakawa H, Hayashi-Takanaka Y, Haraguchi T, Hiraoka Y. \u201cHuman Ebp1 rescues the synthetic lethal growth of fission yeast cells lacking Cdb4 and Nup184\u201d <em>Genes Cells<\/em>, <strong>25(4)<\/strong>: 288-295 (2020) DOI: 10.1111\/gtc.12757<\/li>\n\n\n\n<li>Kinugasa Y, Hirano Y, Sawai M, Ohno Y, Shindo T, Asakawa H, Chikashige Y, Shibata S, Kihara A, Haraguchi T, Hiraoka Y. \u201cThe very-long-chain fatty acid elongase Elo2 rescues lethal defects associated with loss of the nuclear barrier function\u201d <em>J. Cell Sci.<\/em>, <strong>132(10)<\/strong>: jcs229021 (2019) DOI: 10.1242\/jcs.229021<br><mark style=\"background-color:rgba(0, 0, 0, 0);color:#d60000\" class=\"has-inline-color\">Research Highlights\u3067\u7d39\u4ecb\u3055\u308c\u305f<\/mark><\/li>\n\n\n\n<li>Hirano Y, Kinugasa Y, Asakawa H, Chikashige Y, Obuse C. Haraguchi T, Hiraoka Y. \u201cLem2 is retained at the nuclear envelope through its interaction with Bqt4 in fission yeast\u201d <em>Genes Cells<\/em>, <strong>23(3)<\/strong>: 122-135 (2018) DOI: 10.1111\/gtc.12557<br><mark style=\"background-color:rgba(0, 0, 0, 0);color:#de0000\" class=\"has-inline-color\">Top downloaded article 2017-2018 in this journal:a top 20 most read paper\u306b\u9078\u51fa<\/mark><\/li>\n\n\n\n<li>Matsuda A, Schermelleh L, Hirano Y, Haraguchi T, Hiraoka Y. \u201cAccurate and fiducial-marker-free correction for three-dimensional chromatic shift in biological fluorescence microscopy\u201d <em>Sci. Rep.<\/em>, <strong>8(1)<\/strong>:7583 (2018) DOI: 10.1038\/s41598-018-25922-7<br><mark style=\"background-color:rgba(0, 0, 0, 0);color:#d80000\" class=\"has-inline-color\">Top 100 most accessed papers in Cell and Molecular Biology\u306b\u9078\u51fa<\/mark><\/li>\n\n\n\n<li>Hirai Y, Hirano Y, Matsuda A, Hiraoka Y, Honda T, Tomonaga K. \u201cBorna Disease Virus Assembles Porous Cage-like Viral Factories in the Nucleus\u201d <em>J. Biol. Chem.<\/em>, <strong>291(50)<\/strong>: 25789-25798 (2016) DOI: 10.1074\/jbc.M116.746396<\/li>\n\n\n\n<li>Tange Y, Chikashige Y, Takahata S, Kawakami K, Higashi M, Mori C, Kojidani T, Hirano Y, Asakawa H, Murakami Y, Haraguchi T, Hiraoka Y. \u201cInner nuclear membrane protein Lem2 augments heterochromatin formation in response to nutritional conditions\u201d <em>Genes Cells<\/em>,<strong> 21(8)<\/strong>, 812-832 (2016) DOI: 10.1111\/gtc.12385<\/li>\n\n\n\n<li>G\u00f3mez-Saldivar G, Fernandez A, Hirano Y. Mauro M, Lai A, Ayuso C, Haraguchi T, Hiraoka Y, Piano F, Askjaer P. \u201cIdentification of Conserved MEL-28\/ELYS Domains with Essential Roles in Nuclear Assembly and Chromosome Segregation\u201d <em>PLoS Genet.<\/em>, <strong>12(6)<\/strong>: e1006131 (2016) DOI: 10.1371\/journal.pgen.1006131<\/li>\n\n\n\n<li>Hirano Y, Hizume K, Kimura H, Takeyasu K, Haraguchi T, Hiraoka Y. \u201cLamin B receptor recognizes specific modifications of histone H4 in heterochromatin formation\u201d <em>J. Biol. Chem<\/em>., <strong>287(51)<\/strong>, 42654-42663 (2012) DOI: 10.1074\/jbc.M112.397950<\/li>\n\n\n\n<li>Ito S, Tan LJ, Andoh D, Narita T, Seki M, Hirano Y, Narita K, Kuraoka I, Hiraoka Y, Tanaka K. \u201cMMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation\u201d<em>Mol. Cell<\/em>, <strong>27(4)<\/strong>, 632-640 (2010) DOI: 10.1016\/j.molcel.2010.07.029<\/li>\n\n\n\n<li>Hirano Y(*\u8cac\u4efb\u8457\u8005), Iwase Y, Ishii K, Kumeta M, Horigome T, Takeyasu K. \u201cCell cycle-dependent phosphorylation of MAN1\u201d <em>Biochemistry<\/em>, <strong>48(7)<\/strong>, 1636-1643 (2009) DOI: 10.1021\/bi802060v<\/li>\n\n\n\n<li>Hirano Y(*\u8cac\u4efb\u8457\u8005), Ishii K, Kumeta M, Furukawa K, Takeyasu K Horigome T. \u201cProteomic and targeted analytical identification of BXDC1 and EBNA1BP2 as dynamic scaffold proteins in the nucleolus\u201d <em>Genes Cells<\/em>, <strong>14(2)<\/strong>, 155-166 (2009) DOI: 10.1111\/j.1365-2443.2008.01262.x<\/li>\n\n\n\n<li>Ishii K, Hirano Y, Araki N, Oda T, Kumeta M, Takeyasu K, Furukawa K, Horigome T. \u201cNuclear matrix contains novel WD-repeat and disordered-region-rich proteins\u201d <em>FEBS Lett.<\/em>, <strong>582(23-24)<\/strong>, 3515-3519 (2008) DOI: 10.1016\/j.febslet.2008.09.019<\/li>\n\n\n\n<li>Hirano Y(*\u8cac\u4efb\u8457\u8005), Ohniwa RL, Wada C, Yoshimura SH, Takeyasu K. \u201cHuman small G proteins, ObgH1, and ObgH2, participate in the maintenance of mitochondria and nucleolar architectures\u201d <em>Genes Cells<\/em>,<strong> 11(11)<\/strong>, 1295-1304 (2006) DOI: 10.1111\/j.1365-2443.2006.01017.x<\/li>\n\n\n\n<li>Hirano Y, Segawa M, Ouchi FS, Yamakawa Y, Furukawa K, Takeyasu K, Horigome T. \u201cDissociation of emerin from barrier-to-autointegration factor is regulated through mitotic phosphorylation of emerin in Xenopus egg cell-free system\u201d <em>J. Biol. Chem<\/em>., <strong>280(48)<\/strong>, 39925-39933 (2005) DOI: 10.1074\/jbc.M503214200<\/li>\n\n\n\n<li>Miyachi K, Hirano Y, Horigome T, Mimori K, Miyakawa H, Onozuka Y, Shibata M, Hirakata M, Suwa A, Hosaka H, Matsushima S, Komatsu T, Matsushima H, Hankins RW, Fritzler M.J. \u201cAutoantibodies from primary biliary cirrhosis patients with anti-p95c antibodies bind to recombinant p97\/VCP and inhibit in vitro nuclear envelope assembly\u201d <em>Clin. Exp. Immunol.<\/em>, <strong>136(3)<\/strong>, 568-573 (2004) DOI: 10.1111\/j.1365-2249.2004.02456.x<\/li>\n\n\n\n<li>Nakagawa T<sup>#<\/sup>, Hirano Y<sup>#<\/sup>(<sup>#<\/sup>\u5171\u540c\u7b2c\u4e00\u8457\u8005), Inomata A, Yokota S, Miyachi K, Kaneda M, Umeda M, Furukawa K, Omata S, Horigome T. \u201cParticipation of a Fusogenic Protein, Glyceraldehyde-3-Phosphate Dehydrogenase, in Nuclear Membrane Assembly\u201d <em>J. Biol. Chem.<\/em>, <strong>278(22)<\/strong>, 20395-20404 (2003) DOI: 10.1074\/jbc.M210824200<\/li>\n<\/ul>\n\n\n\n<h2 class=\"wp-block-heading\">\u7dcf\u8aac(\u67fb\u8aad\u6709)<\/h2>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Asakawa H, Hirano Y, Haraguchi T. \u201cNuclear Organization (Nuclear Structure and Dynamics)\u201d <em>Encyclopedia of Cell Biology, 2nd Edition<\/em>,<strong> 2<\/strong>, 408-41 (2023)<\/li>\n\n\n\n<li>Hirano Y, Asakawa H, Sakuno T, Haraguchi T, Hiraoka Y. \u201cNuclear Envelope Proteins Modulating the Heterochromatin Formation and Functions in Fission Yeast\u201d <em>Cells<\/em>, <strong>9(8)<\/strong>:E1908 (2020)<\/li>\n\n\n\n<li>Hirano Y, Matsuda A, Hiraoka Y. \u201cRecent advancements in structured-illumination microscopy toward live-cell imaging\u201d <em>Microscopy(Oxf)<\/em>, <strong>64(4)<\/strong>, 237-249 (2015)<\/li>\n\n\n\n<li>Hirano Y, Takahashi H, Kumeta M, Hizume K, Ohtsuka S, Yoshimura SH, Takeyasu K. \u201cNuclear architecture and chromatin dynamics revealed by atomic force microscopy in combination with biochemistry and cell biology\u201d <em>Pflugers Arch.<\/em>, <strong>456(1)<\/strong>, 139-153 (2008)<\/li>\n<\/ul>\n\n\n\n<h2 class=\"wp-block-heading\">\u8457\u66f8<\/h2>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>\u5e73\u91ce\u6cf0\u5f18<\/strong>,\u677e\u7530\u539a\u5fd7,\u5e73\u5ca1\u6cf0\u300c\u5b9f\u8df5\u7de83. 3D-SIM \u306b\u3088\u308b\u7d30\u80de\u5185\u69cb\u9020\u306e\u8d85\u89e3\u50cf\u30a4\u30e1\u30fc\u30b8\u30f3\u30b0\u300d\u521d\u3081\u3066\u3067\u3082\u3067\u304d\u308b!\u8d85\u89e3\u50cf\u30a4\u30e1\u30fc\u30b8\u30f3\u30b0\u3001146-156\u3001\u7f8a\u571f\u793e\u30002016\u5e74<\/li>\n\n\n\n<li>\u677e\u7530\u539a\u5fd7\u3001<strong>\u5e73\u91ce\u6cf0\u5f18<\/strong>\u3001\u5e73\u5ca1\u6cf0\u300c\u539f\u7406\u30fb\u5fdc\u7528\u7de83.\u3000\u69cb\u9020\u5316\u7167\u660e\u9855\u5fae\u93e1\u6cd5SIM\u2015\u7e1e\u7167\u660e\u306e\u3064\u304f\u308b\u30e2\u30a2\u30ec\u304c\u53ef\u80fd\u306b\u3059\u308b\u8d85\u89e3\u50cf\u89b3\u5bdf\u300d\u521d\u3081\u3066\u3067\u3082\u3067\u304d\u308b!\u8d85\u89e3\u50cf\u30a4\u30e1\u30fc\u30b8\u30f3\u30b0 219-228\u3001\u7f8a\u571f\u793e\u30002016\u5e74<\/li>\n\n\n\n<li><strong>\u5e73\u91ce\u6cf0\u5f18<\/strong>\u3001\u677e\u7530\u539a\u5fd7\u300c\u8d85\u5206\u89e3\u86cd\u5149\u9855\u5fae\u93e1\u6cd5\u300d\u65b0\u30fb\u751f\u7d30\u80de\u86cd\u5149\u30a4\u30e1\u30fc\u30b8\u30f3\u30b0\u3001\u7b2c7\u7ae0\u3001\u5171\u7acb\u51fa\u7248\u30002015\u5e74<\/li>\n\n\n\n<li>\u677e\u7530\u539a\u5fd7\u3001\u539f\u53e3\u5fb3\u5b50\u3001<strong>\u5e73\u91ce\u6cf0\u5f18<\/strong>\u300c\u8d85\u9ad8\u5206\u89e3\u86cd\u5149\u9855\u5fae\u93e1\u6cd5=\u89e3\u50cf\u5ea6\u306e\u9650\u754c\u3092\u8d85\u3048\u3066\u898b\u308b=\u300d\u5149\u30a2\u30e9\u30a4\u30a2\u30f3\u30b9\u30013, 31-35\u3001\u65e5\u672c\u5de5\u696d\u51fa\u7248\u30002014\u5e74<\/li>\n\n\n\n<li>\u677e\u7530\u539a\u5fd7\u3001<strong>\u5e73\u91ce\u6cf0\u5f18<\/strong>\u3001\u5e73\u5ca1\u6cf0\u300c\u6838\u5185\u69cb\u9020\u89b3\u5bdf\u306e\u305f\u3081\u306e\u8d85\u5206\u89e3\u80fd\u9855\u5fae\u93e1\u30a4\u30e1\u30fc\u30b8\u30f3\u30b0\u6280\u8853\u300d\u7d30\u80de\u5de5\u5b66\u300131, 863-869\u3001\u5b66\u7814\u30e1\u30c7\u30a3\u30ab\u30eb\u79c0\u6f64\u793e\u30002012\u5e74<\/li>\n\n\n\n<li><strong>\u5e73\u91ce\u6cf0\u5f18<\/strong>\u3001\u5e73\u5ca1\u6cf0\u300c\u30d2\u30b9\u30c8\u30f3H1\u300d\u751f\u4f53\u306e\u5316\u5b66\u300162, 438-439\u3001\u533b\u5b66\u66f8\u9662\u30002011\u5e74<\/li>\n\n\n\n<li><strong>\u5e73\u91ce\u6cf0\u5f18<\/strong>\u3001\u9ad8\u6a4b\u5bdb\u82f1\u3001\u5409\u6751\u6210\u5f18\u3001\u7af9\u5b89\u90a6\u592b\u300c\u539f\u5b50\u9593\u529b\u9855\u5fae\u93e1\u3092\u7528\u3044\u305f\u529b\u5b66\u6e2c\u5b9a\u3068\u5206\u5b50\u8a8d\u8b58\u30a4\u30e1\u30fc\u30b8\u30f3\u30b0\u300d\u751f\u547d\u79d1\u5b66\u8005\u306e\u305f\u3081\u306e\u6a5f\u5668\u5206\u6790\u5b9f\u9a13\u30cf\u30f3\u30c9\u30d6\u30c3\u30af\u3001116-121\u3001\u7f8a\u571f\u793e2007\u5e74<\/li>\n\n\n\n<li>Horigome T, <strong>Hirano Y<\/strong> and Furukawa K \u201cDynamics, roles and diseases of the nuclear membrane, lamins and lamin-binding proteins\u201d Nuclear Dynamics, 123-144, Springer (2007)<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>\u539f\u8457\u8ad6\u6587(Original articles) 2021\u5e74- 2003-2020\u5e74 \u7dcf\u8aac(\u67fb\u8aad\u6709) 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