The Physiological Relevance of Protein Phosphatase 1 and its Interacting Proteins to Health and Disease

2012 ◽  
Vol 17 (33) ◽  
pp. 3996-4017 ◽  
Author(s):  
M. Fardilha ◽  
S. L.C. Esteves ◽  
L. Korrodi-Gregorio ◽  
O. A.B. da Cruz e Silva ◽  
E. F. da Cruz e Silva
2004 ◽  
Vol 327 (2) ◽  
pp. 93-97 ◽  
Author(s):  
Alphonse Garcia ◽  
Xavier Cayla ◽  
Bernard Caudron ◽  
Éric Deveaud ◽  
Fernando Roncal ◽  
...  

2014 ◽  
Vol 164 (5) ◽  
pp. 366-391 ◽  
Author(s):  
Luís Korrodi-Gregório ◽  
Sara L.C. Esteves ◽  
Margarida Fardilha

2021 ◽  
Author(s):  
Juliana Felgueiras ◽  
Luís Sousa ◽  
Ana Luísa Luísa Teixeira ◽  
Bárbara Regadas ◽  
Luís Korrodi-Gregório ◽  
...  

Abstract Protein phosphatase 1 (PP1) regulates several cellular events via interaction with multiple regulatory subunits. The human prostate proteome includes various PP1-interacting proteins; however, a very limited number of interactions is yet characterized and their role in prostate tumorigenesis remains poorly understood. Tctex1 domain-containing protein 4 (TCTEX1D4) was previously identified as a PP1-interacting protein, but its function, as well as the relevance of its interaction with PP1, are virtually unknown. In this study we addressed the role of the PP1/TCTEX1D4 complex in prostate tumorigenesis. We found distinct expression levels and subcellular distributions for TCTEX1D4 and PP1γ in human prostate epithelial normal-like and malignant cells. Moreover, we showed that TCTEX1D4 participates in the regulation of cell proliferation and modulation of microRNAs expression and that its interaction with PP1 controls its function. Taken together, our study provides first evidence for the involvement of the PP1/TCTEX1D4 complex in prostate tumorigenesis.


2017 ◽  
Vol 45 (1) ◽  
pp. 89-99 ◽  
Author(s):  
Iris Verbinnen ◽  
Monica Ferreira ◽  
Mathieu Bollen

Protein phosphatase 1 (PP1) is expressed in all eukaryotic cells and catalyzes a substantial fraction of phosphoserine/threonine dephosphorylation reactions. It forms stable complexes with PP1-interacting proteins (PIPs) that guide the phosphatase throughout its life cycle and control its fate and function. The diversity of PIPs is huge (≈200 in vertebrates), and most of them combine short linear motifs to form large and unique interaction interfaces with PP1. Many PIPs have separate domains for PP1 anchoring, PP1 regulation, substrate recruitment and subcellular targeting, which enable them to direct associated PP1 to a specific subset of substrates and mediate acute activity control. Hence, PP1 functions as the catalytic subunit of a large number of multimeric holoenzymes, each with its own subset of substrates and mechanism(s) of regulation.


Diabetes ◽  
1996 ◽  
Vol 45 (3) ◽  
pp. 322-327 ◽  
Author(s):  
E. D. Crook ◽  
D. A. McClain

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