MISC

2006年5月

A small Ras-like protein Ray/Rab1c modulates the p53-regulating activity of PRPK

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
  • Y Abe
  • ,
  • T Takeuchi
  • ,
  • Y Imai
  • ,
  • R Murase
  • ,
  • Y Kamei
  • ,
  • T Fujibuchi
  • ,
  • S Matsumoto
  • ,
  • N Ueda
  • ,
  • M Ogasawara
  • ,
  • K Shigemoto
  • ,
  • K Kito

344
1
開始ページ
377
終了ページ
385
記述言語
英語
掲載種別
DOI
10.1016/j.bbrc.2006.03.071
出版者・発行元
ACADEMIC PRESS INC ELSEVIER SCIENCE

PRPK phosphorylates serine-15 residue of p53 and enhances transcriptional activity. PRPK possesses a bipartite nuclear localization signal and localizes in nucleus when over-expressed in cells. However, intrinsic PRPK localizes mainly in the cytosol in situ. While studying the mechanisms in the distribution of intrinsic PRPK, we identified a PRPK binding protein, an ubiquitously expressed Small Ras-like GTPase, Rabic, also named Ray or Rab35. The over-expressed Ray was distributed in the nucleus, cytosol.. and cell membrane. Both Ray wild type and GTP-restrictively binding mutant Ray-Q67L, but not guanine nucleotide unstable binding Mutant Ray-N120I, partially distributed the over-expressed PRPK to the cytosol and also Suppressed the PRPK-induced p53-transcriptional activity profoundly. A Small Ras-like GTPase protein Ray was thus indicated to modulate p53 transcriptional activity of PRPK. (c) 2006 Elsevier Inc. All rights reserved.

Web of Science ® 被引用回数 : 16

リンク情報
DOI
https://doi.org/10.1016/j.bbrc.2006.03.071
CiNii Articles
http://ci.nii.ac.jp/naid/80019198329
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/16600182
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000237408000054&DestApp=WOS_CPL