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. 2019 Oct 15;9:1039. doi: 10.3389/fonc.2019.01039

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Copyright © 2019 Simoni-Nieves, Gerardo-Ramírez, Pedraza-Vázquez, Chávez-Rodríguez, Bucio, Souza, Miranda-Labra, Gomez-Quiroz and Gutiérrez-Ruiz.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The signal transduction of GDF11. The figure displays the canonical signal transduction mediated by R-SMAD (SMAD 2/3, SMAD 1,5,8), assisted by the Co-SMAD (SMAD4). The signal could inhibited by inhibitory SMAD (I-SMAD) 6 or 7 or by the SMAD specific E3 ubiquitin protein ligase (SMURF). Extracellularly, GDF11 could be inhibited by the BMP and activin membrane-bound inhibitor (BAMBI), or the action of proteins such as Follistatin, Decorin, and GDF-associated serum protein-1 (GASP-1) and GASP-2. The non-canonical pathway is driven particularly by the Mitogen Activated Proteins Kinases (MAPK), signaling continues to the tumor necrosis factor receptor-associated factor (TRAF) 2 or 6; and TGF-β activated kinase 1 (TAK1), which in addition uses the TAK1 binding protein (TAB) 1 and one of both 2 or 3. Non-canonical regulation could influence the nuclear factor kappa B (NF-kB) among others, and the inhibition of this pathway could be blocked by protein phosphatases (PP).