論文

査読有り
2015年7月

Nucleus accumbens associated 1 is recruited within the promyelocytic leukemia nuclear body through SUMO modification

CANCER SCIENCE
  • Yoshinori Tatemichi
  • ,
  • Masahiko Shibazaki
  • ,
  • Shinji Yasuhira
  • ,
  • Shuya Kasai
  • ,
  • Hiroshi Tada
  • ,
  • Hiroki Oikawa
  • ,
  • Yuji Suzuki
  • ,
  • Yasuhiro Takikawa
  • ,
  • Tomoyuki Masuda
  • ,
  • Chihaya Maesawa

106
7
開始ページ
848
終了ページ
856
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1111/cas.12680
出版者・発行元
WILEY-BLACKWELL

Nucleus accumbens associated 1 (NACC1) is a cancer-associated BTB/POZ (pox virus and zinc finger/bric-a-brac tramtrack broad complex) gene, and is involved in several cellular functions in neurons, cancer and stem cells. Some of the BTB/POZ proteins associated with cancer biology are SUMOylated, which appears to play an important role in transcription regulation. We show that NACC1 is SUMOylated on a phylogenetically conserved lysine (K167) out of three consensus SUMOylation motif sites. Amino acid substitution in the SIM sequence (SIM/M) within the BTB/POZ domain partially reduced K167 SUMOylation activity of NACC1. Overexpression of GFP-NACC1 fusion protein leads to formation of discrete nuclear foci similar to promyelocytic leukemia nuclear bodies (PML-NB), which colocalized with SUMO paralogues (SUMO1/2/3). Both NACC1 nuclear body formation and colocalization with SUMO paralogues were completely suppressed in the GFP-NACC1-SIM/M mutant, whereas they were partially maintained in the NACC1 K167R mutant. Confocal immunofluorescence analysis showed that endogenous and exogenous NACC1 proteins colocalized with endogenous PML protein. A pull-down assay revealed that the consensus motifs of the SUMO acceptor site at K167 and the SIM within the BTB/POZ domain were both necessary for efficient binding to PML protein. Our study demonstrates that NACC1 can be modified by SUMO paralogues, and cooperates with PML protein.

Web of Science ® 被引用回数 : 3

リンク情報
DOI
https://doi.org/10.1111/cas.12680
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000357883900009&DestApp=WOS_CPL

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