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. 2006 May 26;344(1):377-85.
doi: 10.1016/j.bbrc.2006.03.071. Epub 2006 Mar 22.

A Small Ras-like Protein Ray/Rab1c Modulates the p53-regulating Activity of PRPK

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A Small Ras-like Protein Ray/Rab1c Modulates the p53-regulating Activity of PRPK

Yasuhito Abe et al. Biochem Biophys Res Commun. .

Abstract

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, Rab1c, 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.

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