TY - JOUR
T1 - Post-translational modifications of the TAK1-TAB complex
AU - Hirata, Yusuke
AU - Takahashi, Miki
AU - Morishita, Tohru
AU - Noguchi, Takuya
AU - Matsuzawa, Atsushi
N1 - Funding Information:
We thank all members of Lab of Health Chemistry for helpful discussions. This work was supported by KAKENHI from the Japan Society for the Promotion of Science (JSPS) and the Ministry of Education, Culture, Sports, Science and Technology (NEXT).
Publisher Copyright:
© 2017 by the authors; licensee MDPI, Basel, Switzerland.
PY - 2017/1/19
Y1 - 2017/1/19
N2 - Transforming growth factor-β (TGF-β)-activated kinase 1 (TAK1) is a member of the mitogen-activated protein kinase kinase kinase (MAPKKK) family that is activated by growth factors and cytokines such as TGF-β, IL-1β, and TNF-α, and mediates a wide range of biological processes through activation of the nuclear factor-κB (NF-κB) and the mitogen-activated protein (MAP) kinase signaling pathways. It is well established that activation status of TAK1 is tightly regulated by forming a complex with its binding partners, TAK1-binding proteins (TAB1, TAB2, and TAB3). Interestingly, recent evidence indicates the importance of post-translational modifications (PTMs) of TAK1 and TABs in the regulation of TAK1 activation. To date, a number of PTMs of TAK1 and TABs have been revealed, and these PTMs appear to fine-tune and coordinate TAK1 activities depending on the cellular context. This review therefore focuses on recent advances in the understanding of the PTMs of the TAK1-TAB complex.
AB - Transforming growth factor-β (TGF-β)-activated kinase 1 (TAK1) is a member of the mitogen-activated protein kinase kinase kinase (MAPKKK) family that is activated by growth factors and cytokines such as TGF-β, IL-1β, and TNF-α, and mediates a wide range of biological processes through activation of the nuclear factor-κB (NF-κB) and the mitogen-activated protein (MAP) kinase signaling pathways. It is well established that activation status of TAK1 is tightly regulated by forming a complex with its binding partners, TAK1-binding proteins (TAB1, TAB2, and TAB3). Interestingly, recent evidence indicates the importance of post-translational modifications (PTMs) of TAK1 and TABs in the regulation of TAK1 activation. To date, a number of PTMs of TAK1 and TABs have been revealed, and these PTMs appear to fine-tune and coordinate TAK1 activities depending on the cellular context. This review therefore focuses on recent advances in the understanding of the PTMs of the TAK1-TAB complex.
KW - MAP kinase
KW - NF-κB
KW - Post-translational modification
KW - TAB1
KW - TAB2
KW - TAB3
KW - TAK1
UR - http://www.scopus.com/inward/record.url?scp=85010777979&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85010777979&partnerID=8YFLogxK
U2 - 10.3390/ijms18010205
DO - 10.3390/ijms18010205
M3 - Review article
C2 - 28106845
AN - SCOPUS:85010777979
SN - 1422-0067
VL - 18
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
IS - 1
M1 - 205
ER -