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Protein phosphatase PP1‐NIPP1 activates mesenchymal genes in HeLa cells
Author(s) -
Van Dessel Nele,
Boens Shannah,
Lesage Bart,
Winkler Claudia,
Görnemann Janina,
Van Eynde Aleyde,
Bollen Mathieu
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.04.017
Subject(s) - filopodia , biology , protein phosphatase 1 , microbiology and biotechnology , dephosphorylation , gastrulation , phosphorylation , phosphatase , actin , mesenchymal stem cell , chemistry , embryo , embryogenesis
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.

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