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GLTSCR2 is an upstream negative regulator of nucleophosmin in cervical cancer.

Abstract
Nucleophosmin (NPM)/B23, a multifunctional nucleolar phosphoprotein, plays an important role in ribosome biogenesis, cell cycle regulation, apoptosis and cancer pathogenesis. The role of NPM in cells is determined by several factors, including total expression level, oligomerization or phosphorylation status, and subcellular localization. In the nucleolus, NPM participates in rRNA maturation to enhance ribosomal biogenesis. Consistent with this finding, NPM expression is increased in rapidly proliferating cells and many types of human cancers. In response to ribosomal stress, NPM is redistributed to the nucleoplasm, where it inactivates mouse double minute 2 homologue to stabilize p53 and inhibit cell cycle progression. These observations indicate that nucleolus-nucleoplasmic mobilization of NPM is one of the key molecular mechanisms that determine the role of NPM within the cell. However, the regulatory molecule(s) that control(s) NPM stability and subcellular localization, crucial to the pluripotency of intercellular NPM, remain(s) unidentified. In this study, we showed that nucleolar protein GLTSCR2/Pict-1 induced nucleoplasmic translocation and enhanced the degradation of NPM via the proteasomal polyubiquitination pathway. In addition, we showed that GLTSCR2 expression decreased the transforming activity of cells mediated by NPM and that the expression of NPM is reciprocally related to that of GLTSCR2 in cervical cancer tissue. In this study, we demonstrated that GLTSCR2 is an upstream negative regulator of NPM.
AuthorsJee-Youn Kim, Young-Eun Cho, Yong-Min An, Sang-Hoon Kim, Yong-Gwan Lee, Jae-Hoon Park, Sun Lee
JournalJournal of cellular and molecular medicine (J Cell Mol Med) Vol. 19 Issue 6 Pg. 1245-52 (Jun 2015) ISSN: 1582-4934 [Electronic] England
PMID25818168 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Copyright© 2015 The Authors. Journal of Cellular and Molecular Medicine published by John Wiley & Sons Ltd and Foundation for Cellular and Molecular Medicine.
Chemical References
  • NOP53 protein, human
  • NPM1 protein, human
  • Npm1 protein, mouse
  • Nuclear Proteins
  • Tumor Suppressor Proteins
  • Nucleophosmin
  • Proteasome Endopeptidase Complex
Topics
  • Blotting, Western
  • Cell Nucleolus (metabolism)
  • Cell Nucleus (metabolism)
  • Down-Regulation
  • Female
  • HeLa Cells
  • Humans
  • Immunohistochemistry
  • Nuclear Proteins (metabolism)
  • Nucleophosmin
  • Proteasome Endopeptidase Complex (metabolism)
  • Protein Stability
  • Protein Transport
  • Proteolysis
  • RNA Interference
  • Signal Transduction
  • Tumor Suppressor Proteins (genetics, metabolism)
  • Ubiquitination
  • Uterine Cervical Neoplasms (metabolism, pathology)

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