◀ Back to MAPK14

MAPK14 — TAB1

Pathways - manually collected, often from reviews:

• KEGG NOD-like receptor signaling pathway: Complex of MAP3K7-TAB1-TAB2-TAB3 → MAPK11/MAPK12/MAPK13/MAPK14 (protein-protein, activation)
  
• NCI Pathway Database Regulation of p38-alpha and p38-beta: TAB1 (TAB1) → PGK/cGMP/p38 alpha complex (PRKG1-MAPK14) (modification, collaborate)
  Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
  Evidence: mutant phenotype, assay, physical interaction, other species
• NCI Pathway Database Regulation of p38-alpha and p38-beta: TAB1 (TAB1) → p38 alpha (MAPK14) (modification, collaborate) Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
  Evidence: mutant phenotype, assay, physical interaction, other species
• NCI Pathway Database Regulation of p38-alpha and p38-beta: TAB1 (TAB1) → p38 alpha/TAB1 complex (MAPK14-TAB1) (modification, collaborate)
  Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
  Evidence: mutant phenotype, assay, physical interaction, other species
• NCI Pathway Database Regulation of p38-alpha and p38-beta: PGK/cGMP/p38 alpha complex (PRKG1-MAPK14) → p38 alpha/TAB1 complex (MAPK14-TAB1) (modification, collaborate)
  Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
  Evidence: mutant phenotype, assay, physical interaction, other species
• NCI Pathway Database Regulation of p38-alpha and p38-beta: PGK/cGMP complex (PRKG1) → p38 alpha/TAB1 complex (MAPK14-TAB1) (modification, collaborate)
  Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
  Evidence: mutant phenotype, assay, physical interaction, other species
• NCI Pathway Database Regulation of p38-alpha and p38-beta: p38 alpha (MAPK14) → p38 alpha/TAB1 complex (MAPK14-TAB1) (modification, collaborate)
  Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
  Evidence: mutant phenotype, assay, physical interaction, other species
• NCI Pathway Database p38 MAPK signaling pathway: TAB family (TAB2/TAB1) → p38alpha-beta-active (MAPK14/MAPK11) (modification, collaborate)
  Wang et al., Nature 2001, Cheung et al., EMBO J 2003, Shibuya et al., Science 1996
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database p38 MAPK signaling pathway: p38alpha-beta-active (MAPK14/MAPK11) → TAK1/TAB family complex (MAP3K7-TAB2_TAB1) (modification, inhibits)
  Wang et al., Nature 2001, Cheung et al., EMBO J 2003, Shibuya et al., Science 1996
  Evidence: mutant phenotype, physical interaction

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind_translation Interaction: TAB1 — MAPK14 (coimmunoprecipitation) Tanno et al., Circ Res 2003*
• IRef Biogrid Interaction: TAB1 — MAPK14 (physical association, affinity chromatography technology) Ge et al., Science 2002*
• IRef Biogrid Interaction: TAB1 — MAPK14 (direct interaction, two hybrid) Vinayagam et al., Science signaling 2011
• IRef Biogrid Interaction: TAB1 — MAPK14 (physical association, affinity chromatography technology) Ge et al., J Biol Chem 2003*
• IRef Biogrid Interaction: TAB1 — MAPK14 (direct interaction, pull down) Ge et al., Science 2002*
• IRef Hprd Interaction: MAPK14 — TAB1 (in vitro) Ge et al., Science 2002*
• IRef Hprd Interaction: Complex of MAPK14-TAB1-MAPK14-TRAF6-TRAF6-TRAF6-TAB1-MAPK14-TAB1 (in vivo) Ge et al., Science 2002*
• IRef Intact Interaction: TAB1 — MAPK14 (physical association, coimmunoprecipitation) Ge et al., Science 2002*
• IRef Intact Interaction: TAB1 — MAPK14 (physical association, two hybrid) Ge et al., Science 2002*
• IRef Intact Interaction: TAB1 — MAPK14 (physical association, two hybrid) Vinayagam et al., Science signaling 2011
• IRef Ophid Interaction: TAB1 — MAPK14 (aggregation, confirmational text mining) Ge et al., Science 2002*
• IRef Ophid Interaction: TAB1 — MAPK14 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

McDermott et al., J Biol Chem 2002 : In addition we found a role for TAK-1 in the activation of p38 MAPK by IL-1, with TAK-1 also associating with active Ras
Cheung et al., EMBO J 2003 : Our results suggest that TAB1 participates in a SAPK2a/p38alpha mediated feedback control of TAK1 , which not only limits the activation of SAPK2a/p38alpha but synchronizes its activity with other signalling pathways that lie downstream of TAK1 ( JNK and IKK )
Cheung et al., Biochem J 2004 : The SAPK2a/p38alpha mediated phosphorylation of TAB2 and TAB3 may contribute to the SAPK2a/p38alpha mediated feedback control of TAK1 activity that also involves the phosphorylation of TAB1
Singhirunnusorn et al., J Biol Chem 2005 : Furthermore, SB203580 and p38alpha small interfering RNA enhanced TNF-alpha induced Thr-187 phosphorylation as well as TAK1 kinase activity, indicating that the phosphorylation is affected by p38alpha/TAB1/TAB2 mediated feedback control of TAK1
Makeeva et al., International journal of biological sciences 2007 : The aim of present study was to elucidate the role of TAB1 in nitric oxide induced activation of p38 MAPK
Kim et al., American journal of physiology. Renal physiology 2007 : TGF-beta activated kinase 1 and TAK1 binding protein 1 cooperate to mediate TGF-beta1 induced MKK3-p38 MAPK activation and stimulation of type I collagen
Windheim et al., Biochem J 2007 : We also show that RIP2 induces the activation of the protein kinase TAK1 ( transforming-growth-factor-beta activated kinase-1 ), that a dominant negative mutant of TAK1 inhibits RIP2 induced activation of JNK ( c-Jun N-terminal kinase ) and p38alpha MAPK , and that signalling downstream of NOD2 or RIP2 is reduced by the TAK1 inhibitor ( 5Z ) -7-oxozeaenol or in TAK1-deficient cells
Makeeva et al., Endocrinology 2008 : Transforming growth factor-beta activated protein kinase 1-binding protein ( TAB)-1alpha , but not TAB1beta, mediates cytokine induced p38 mitogen activated protein kinase phosphorylation and cell death in insulin producing cells ... Transforming growth factor-beta activated protein kinase 1-binding protein ( TAB)-1alpha, but not TAB1beta , mediates cytokine induced p38 mitogen activated protein kinase phosphorylation and cell death in insulin producing cells
Mendoza et al., Biochem J 2008 : Studies using TAB1 ( -/- ) MEFs indicate important roles for TAB1 in recruiting p38alpha MAPK to the TAK1 complex for the phosphorylation of TAB3 at Ser ( 60 ) and Thr ( 404 ) and in inhibiting the dephosphorylation of TAB3 at Ser ( 506 )
Kodym et al., RNA 2008 (MAP Kinase Signaling System) : Activation of TAK1-D leads to the downstream activation of the p38 MAPK and of SAPK/JNK but not the NFkappaB pathway
Mikkelsen et al., J Biol Chem 2009 : We also observed that TRAF2 and TAK1 were essential for RIG-I mediated activation of p38 MAPK
Cheng et al., J Biomed Mater Res A 2010 (Inflammation...) : The critical role for TAK1 in p38MAPK and NFkappaB activation was as well confirmed by the inhibition of p38MAPK and NFkappaB activity following 5Z-7-oxozeaenol, a selective inhibitor of TAK1
Wolf et al., PloS one 2011 : The TAB1 mutant lacking aa 452-457 decreases TAB1 dependent phosphorylation of p38 MAPK
Tran et al., J Biol Chem 2012 (MAP Kinase Signaling System) : In agreement with this, overexpression of ASK1 or TAK1 resulted in enhanced p38MAPK activation, and their knockdown inhibited p38MAPK in C2C12 cells
Yumoto et al., J Biol Chem 2013 (Cleft Palate) : Our studies show that in neural crest derived craniofacial ecto-mesenchymal cells, Tak1 is not only required for TGF-ß- and bone morphogenetic protein induced p38 Mapk activation but also plays a role in agonist induced C-terminal and linker region phosphorylation of the receptor mediated R-Smads