Genes to Cells

Cover image for Vol. 22 Issue 1

Early View (Online Version of Record published before inclusion in an issue)

Edited By: Mitsuhiro Yanagida

Impact Factor: 2.481

ISI Journal Citation Reports © Ranking: 2015: 85/166 (Genetics & Heredity); 123/187 (Cell Biology)

Online ISSN: 1365-2443

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  1. 1 - 6
  1. Original Articles

    1. Immature Core protein of hepatitis C virus induces an unfolded protein response through inhibition of ERAD-L in a yeast model system

      Shota Takahashi, Naoko Sato, Junichi Kikuchi, Hideaki Kakinuma, Jun Okawa, Yukiko Masuyama, Singo Iwasa, Hayato Irokawa, Gi-Wook Hwang, Akira Naganuma, Michinori Kohara and Shusuke Kuge

      Version of Record online: 18 JAN 2017 | DOI: 10.1111/gtc.12464

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      Structural protein Core of hepatitis C virus (HCV), a cytosolic protein, induces endoplasmic reticulum (ER) stress and unfolded protein response (UPR) in hepatocytes, and is responsible for the pathogenesis of persistent HCV infection. Utilizing yeast as a model system, we found that the immature Core inhibits ERAD-L, a degradation system responsible for misfolded/unfolded proteins in the ER lumen, and induces UPR. Requirement of an unfolded protein sensor in the ER lumen suggested that inhibition of ERAD-L is probably responsible for Core-dependent UPR activation.

    2. In situ electrical monitoring of cancer cells invading vascular endothelial cells with semiconductor-based biosensor

      Toshiya Sakata and Yusuke Matsuse

      Version of Record online: 18 JAN 2017 | DOI: 10.1111/gtc.12473

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      Cellular dynamics is very closely related to ionic behaviors, most of which have been hardly monitored in real time, whereas semiconductor-based biosensors have the unique advantage of direct detection of ionic charges in a real-time and noninvasive manner. In this study, we monitored the invasion process of cancer cells into the vascular endothelial layer in real time by a label-free method using a field-effect transistor (FET) biosensor.

    3. Activin A in combination with ERK1/2 MAPK pathway inhibition sustains propagation of mouse embryonic stem cells

      Yuhei Ashida, May Nakajima-Koyama, Akira Hirota, Takuya Yamamoto and Eisuke Nishida

      Version of Record online: 18 JAN 2017 | DOI: 10.1111/gtc.12467

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      Activin A has an ability to efficiently propagate ESCs when combined with a MEK inhibitor PD0325901. ESCs cultured in Activin+PD show naive pluripotency features, including the gene expression profile, the preferential usage of the Oct4 distal enhancer, and the self-renewal response to Wnt signaling pathway activation.

  2. Brief Reports

    1. Secretome analysis to elucidate metalloprotease-dependent ectodomain shedding of glycoproteins during neuronal differentiation

      Kazuya Tsumagari, Kyoko Shirakabe, Mayu Ogura, Fuminori Sato, Yasushi Ishihama and Atsuko Sehara-Fujisawa

      Version of Record online: 13 JAN 2017 | DOI: 10.1111/gtc.12466

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      We succeeded in the establishment of a sensitive and reliable method to systematically screen glycoproteins that are secreted from differentiating neurons through metalloprotease-dependent ectodomain shedding. Our results show the landscape of ectodomain shedding in differentiating neurons, which should help elucidate the mechanisms of neurogenesis and the pathogeneses of neurological disorders.

  3. Original Articles

    1. Novel tRNA function in amino acid sensing of yeast Tor complex1

      Yoshiaki Kamada

      Version of Record online: 13 JAN 2017 | DOI: 10.1111/gtc.12462

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      Tor complex1 (TORC1) plays a pivotal role in amino acid sensing. In this study, I found that tRNA regulates TORC1. Based on the results, model of tRNA-mediated TORC1 regulation is proposed.

    2. You have full text access to this OnlineOpen article
      Functional mutations in spike glycoprotein of Zaire ebolavirus associated with an increase in infection efficiency

      Mahoko Takahashi Ueda, Yohei Kurosaki, Taisuke Izumi, Yusuke Nakano, Olamide K. Oloniniyi, Jiro Yasuda, Yoshio Koyanagi, Kei Sato and So Nakagawa

      Version of Record online: 13 JAN 2017 | DOI: 10.1111/gtc.12463

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      Analyzing all available Zaire ebolavirus glycoprotein sequences, we found that A82V mutant was fixed in the 2014–2015 outbreak, whereas T544I was not, both of which are under positive selection. Pseudotype assays demonstrated that the A82V mutation caused a small increase in viral infectivity compared with the T544I mutation. Our findings suggest that a driving force for Ebola virus evolution via glycoprotein may be a balance between costs and benefits of its virulence.

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