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Protein phosphatase PP1-NIPP1 activates mesenchymal genes in HeLa cells.
- Source :
-
FEBS letters [FEBS Lett] 2015 May 22; Vol. 589 (12), pp. 1314-21. Date of Electronic Publication: 2015 Apr 20. - Publication Year :
- 2015
-
Abstract
- The deletion of the protein phosphatase-1 (PP1) regulator known as Nuclear Inhibitor of PP1 (NIPP1) is embryonic lethal during gastrulation, hinting at a key role of PP1-NIPP1 in lineage specification. Consistent with this notion we show here that a mild, stable overexpression of NIPP1 in HeLa cells caused a massive induction of genes of the mesenchymal lineage, in particular smooth/cardiac-muscle and matrix markers. This reprogramming was associated with the formation of actin-based stress fibers and retracting filopodia, and a reduced proliferation potential. The NIPP1-induced mesenchymal transition required functional substrate and PP1-binding domains, suggesting that it involves the selective dephosphorylation of substrates of PP1-NIPP1.<br /> (Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Binding Sites
Biomarkers metabolism
Cell Proliferation
Cell Transdifferentiation
Endoribonucleases chemistry
Endoribonucleases genetics
HeLa Cells
Humans
Ligands
Mutation
Neoplasm Proteins chemistry
Neoplasm Proteins genetics
Phosphoprotein Phosphatases chemistry
Phosphoprotein Phosphatases genetics
Phosphorylation
Protein Interaction Domains and Motifs
Protein Stability
RNA-Binding Proteins chemistry
RNA-Binding Proteins genetics
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins metabolism
Endoribonucleases metabolism
Epithelial-Mesenchymal Transition
Gene Expression Regulation, Neoplastic
Genes, Neoplasm
Neoplasm Proteins metabolism
Phosphoprotein Phosphatases metabolism
Protein Processing, Post-Translational
RNA-Binding Proteins metabolism
Transcriptional Activation
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 589
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 25907536
- Full Text :
- https://doi.org/10.1016/j.febslet.2015.04.017