Post-Translational Modifications of the TAK1-TAB Complex
Yusuke Hirata1, Miki Takahashi2, Tohru Morishita3
1Laboratory of Health Chemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai 980-8578, Japan. y-hirata@m.tohoku.ac.jp.
International Journal of Molecular Sciences
|January 21, 2017
Summary
Transforming growth factor-β (TGF-β)-activated kinase 1 (TAK1) and its binding partners (TABs) regulate key cellular processes. Recent research highlights how post-translational modifications (PTMs) fine-tune TAK1-TAB complex activity.
Area of Science:
- Cellular signaling pathways
- Molecular biology
- Signal transduction
Background:
- Transforming growth factor-β (TGF-β)-activated kinase 1 (TAK1) is a MAPKKK family member.
- TAK1 mediates biological processes via NF-κB and MAP kinase pathways.
- TAK1 activation is regulated by binding partners TAB1, TAB2, and TAB3.
Purpose of the Study:
- To review recent advances in understanding post-translational modifications (PTMs) of the TAK1-TAB complex.
- To explore how PTMs regulate TAK1 activation and function.
- To highlight the importance of PTMs in coordinating TAK1 activities.
Main Methods:
- Literature review of recent studies on TAK1 and TAB PTMs.
- Analysis of published data on the functional consequences of TAK1 and TAB modifications.
- Synthesis of current knowledge on PTMs in the TAK1-TAB signaling network.
Main Results:
- Multiple PTMs of TAK1 and TAB proteins have been identified.
- These PTMs play crucial roles in modulating TAK1 kinase activity.
- PTMs fine-tune TAK1-TAB complex function in a context-dependent manner.
Conclusions:
- Post-translational modifications are critical regulators of TAK1-TAB complex signaling.
- Understanding TAK1 PTMs offers insights into cellular responses to growth factors and cytokines.
- Further research into TAK1 PTMs may reveal therapeutic targets for related diseases.
More Related Videos
Related Concept Videos
Covalently Linked Protein Regulators
9.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
9.9K
TGF - β Signaling Pathway
10.8K
The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
10.8K
PI3K/mTOR/AKT Signaling Pathway
6.1K
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a...
6.1K
Phosphorylation
55.1K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
55.1K
Tail-anchoring of Proteins in the ER Membrane
4.0K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
4.0K
MAPK Signaling Cascades
8.9K
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
8.9K


