scholarly journals Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor‐β pathway

2012 ◽  
Vol 24 (11) ◽  
pp. 1999-2006 ◽  
Author(s):  
David L. Bruce ◽  
Thomas Macartney ◽  
Weidong Yong ◽  
Weinian Shou ◽  
Gopal P. Sapkota
Keyword(s):  
Growth Factor ◽  
Protein Phosphatase ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Protein Phosphatase 5

scholarly journals The Cellular Senescence-Inhibited Gene Is Essential for PPM1A Myristoylation To Modulate Transforming Growth Factor β Signaling

2018 ◽  
Vol 38 (23) ◽  
Author(s):  
Feng Zhu ◽  
Nan Xie ◽  
Zhe Jiang ◽  
Guodong Li ◽  
Liwei Ma ◽  
...  
Keyword(s):  
Growth Factor ◽  
Phosphatase Activity ◽  
Cellular Senescence ◽  
Protein Phosphatase ◽  
Transforming Growth Factor ◽  
Regulatory Mechanism ◽  
Biological Significance ◽  
Transforming Growth Factor Β ◽  
Biological Processes ◽  
New Ideas

ABSTRACT The cellular senescence-inhibited gene (CSIG) is implicated in important biological processes, including cellular senescence and apoptosis. Our work showed that CSIG is involved in the myristoylation of the serine/threonine protein phosphatase PPM1A. Previous research has shown that myristoylation is necessary for PPM1A to dephosphorylate Smad2 and Smad3. However, the control and the biological significance of the myristoylation remain poorly understood. In this study, we found that CSIG knockdown disturbs PPM1A myristoylation and reduces the dephosphorylation by PPM1A of its substrate Smad2. By regulating PPM1A myristoylation, CSIG is involved in modulating the signaling of transforming growth factor β (TGF-β). Further study of the mechanism indicated that CSIG facilitates the interaction between N-myristoyltransferase 1 (NMT1) and PPM1A. Taking the data together, we found that CSIG is a regulator of PPM1A myristoylation and TGF-β signaling. By promoting the myristoylation of PPM1A, CSIG enhanced the phosphatase activity of PPM1A and further inhibited TGF-β signaling. This work not only extends the biological significance of CSIG but also provides new ideas and a reference for the study of the regulatory mechanism of myristoylation.

scholarly journals Physical and Functional Interactions between Type I Transforming Growth Factor β Receptors and Bα, a WD-40 Repeat Subunit of Phosphatase 2A

1998 ◽  
Vol 18 (11) ◽  
pp. 6595-6604 ◽  
Author(s):  
Irene Griswold-Prenner ◽  
Craig Kamibayashi ◽  
E. Miko Maruoka ◽  
Marc C. Mumby ◽  
Rik Derynck
Keyword(s):  
Growth Factor ◽  
Protein Phosphatase ◽  
Transforming Growth Factor ◽  
Protein Phosphatase 2A ◽  
Transforming Growth Factor Β ◽  
Type I ◽  
Type Ii ◽  
Functional Interactions ◽  
Phosphatase 2A ◽  
Β Receptor

ABSTRACT We have previously shown that a WD-40 repeat protein, TRIP-1, associates with the type II transforming growth factor β (TGF-β) receptor. In this report, we show that another WD-40 repeat protein, the Bα subunit of protein phosphatase 2A, associates with the cytoplasmic domain of type I TGF-β receptors. This association depends on the kinase activity of the type I receptor, is increased by coexpression of the type II receptor, which is known to phosphorylate and activate the type I receptor, and allows the type I receptor to phosphorylate Bα. Furthermore, Bα enhances the growth inhibition activity of TGF-β in a receptor-dependent manner. Because Bα has been characterized as a regulator of phosphatase 2A activity, our observations suggest possible functional interactions between the TGF-β receptor complex and the regulation of protein phosphatase 2A.

Perianale Fisteln bei CED: vom Mausmodell zur Klinik

2018 ◽  
Vol 75 (5) ◽  
pp. 287-294
Author(s):  
Michael Scharl
Keyword(s):  
Growth Factor ◽  
Morbus Crohn ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Interleukin 13

Zusammenfassung. Fisteln stellen nach wie vor eine der wichtigsten Komplikationen bei Patienten mit Morbus Crohn dar. Bei mindestens einem Drittel aller Morbus Crohn Patienten treten im Laufe der Erkrankung Fisteln auf. Eine dauerhafte Heilung der Fistel wird jedoch, auch unter Ausschöpfung sämtlicher medikamentöser und chirurgischer Therapieoptionen, nur in rund einem Drittel dieser Patienten erreicht. Der genaue molekulare Mechanismus der Fistelentstehung ist bis heute nicht ganz klar. Aus histopathologischer Sichtweise stellen Fisteln eine röhrenartige Struktur dar, welche von flachen epithelartigen Zellen ausgekleidet ist. Als ursächlicher Entstehungsmechanismus wird dabei die sogenannte epitheliale-zu-mesenchymale Transition (EMT) angesehen und es kann eine starke Expression der Entzündungsmediatoren Tumor Nekrose Faktor, Interleukin-13 und Transforming Growth Factor β in den Fistelarealen nachgewiesen werden. Zusätzlich zu den bereits etablierten, medikamentösen Therapieoptionen, also Antibiotika, Immunmodulatoren und anti-TNF Antikörper, stellt insbesondere der Einsatz der mesenchymalen Stammzelltherapie einen erfolgversprechenden Therapieansatz für die Zukunft dar.

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