Human keratinocyte HaCaT cells form aggregates containing Ras-GAP SH3 domain-binding proteins in the cytoplasm in response to a low dose of teniposide Human keratinocyte HaCaT cells form aggregates containing Ras-GAP SH3 domain-binding proteins in the cytoplasm in response to a low dose of teniposide

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Author(s)

    • Qiu Wenzhe
    • Department of Medical Biochemistry, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University
    • Arimoto-Matsuzaki Kyoko
    • Department of Medical Biochemistry, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University
    • Kitamura Masami
    • Department of Medical Biochemistry, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University|Diversity Diamond Unit Project Department, Student Support and Health Administration Organization, Tokyo Medical and Dental University
    • Hata Yutaka
    • Department of Medical Biochemistry, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University|Center for Brain Integration Research, Tokyo Medical and Dental University

Abstract

Eukaryotic cells, when exposed to stress, stopprotein translation and form cytoplasmic granulescalled stress granules (SGs) containing mRNAsand mRNA-binding proteins such as Ras-GAP SH3domain-binding protein (G3BP) 1 and 2. Cells arethought to survive stress by utilizing SGs as theplatform of RNA triage. Accordingly, in cancercells, SGs are proposed to cause resistanceagainst anti-cancer drugs. We initiated this studyto identify novel compounds that induce SGs.We exposed human keratinocyte HaCaT cells tovarious chemical compounds and immunostainedthem with anti-G3BP antibody. We found thatthe cells exposed to topoisomerase inhibitors,teniposide and topotecan, form G3BP-containingaggregates (GCAs). GCAs look like SGs, but areformed more slowly and are not dissociated afterstress removal. GCA formation is not associatedwith eIF2α phosphorylation, while in most cases SGformation depends on it. More importantly, GCAsdo not contain representative components of SGsor mRNAs. In sum, we have unexpectedly found anovel cytoplasmic structure containing G3BP thatis distinct from SG.

Journal

  • Journal of Medical and Dental Sciences

    Journal of Medical and Dental Sciences 66(2), 23-30, 2019

    Tokyo Medical and Dental University

Codes

  • NII Article ID (NAID)
    130007666432
  • Text Lang
    ENG
  • Article Type
    journal article
  • ISSN
    1342-8810
  • Data Source
    IR  J-STAGE 
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