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TNFSF11 — TRAF6

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

Studies that report less than 10 interactions are marked with *

• IRef Hprd Interaction: Complex of 19 proteins (in vivo) Wong et al., Mol Cell 1999
• IRef Hprd Interaction: TNFSF11 — TRAF6 (in vitro) Wong et al., Mol Cell 1999
• IRef Hprd Interaction: TNFSF11 — TRAF6 (in vivo) Wong et al., Mol Cell 1999
• IRef Ophid Interaction: TNFSF11 — TRAF6 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Zhang et al., J Immunol 2003 : Furthermore compared with controls, RANKL induces enhanced association of TRAF6 and RANK in both RAW264.7 cells expressing SHP-1 ( C453S ) and bone marrow macrophages from Me ( v ) /Me ( v ) mice
Takada et al., Blood 2004 : We also found that tumor necrosis factor (TNF) receptor associated factor 6 ( TRAF6 ), which mediates RANKL signaling, was constitutively bound to RANK in TNF receptor deleted cells but not in wild-type cells, and this binding was enhanced by RANKL
Takatsuna et al., J Bone Miner Res 2005 (Bone Resorption) : Interestingly, ( - ) -DHMEQ specifically inhibited the RANKL induced expression of NFATc1 but not the expressions of TRAF6 or c-fos
Takayanagi et al., J Mol Med (Berl) 2005 : RANKL activates TRAF6 , c-Fos, and calcium signaling pathways, all of which are indispensable for the induction and activation of nuclear factor of activated T cells ( NFAT) c1, the master transcription factor for osteoclastogenesis
Poblenz et al., Biochem Biophys Res Commun 2007 (Bone Resorption) : A cell-permeable TRAF6 decoy peptide (T6DP) was shown to specifically target TRAF6 and inhibit RANKL mediated signaling
Bai et al., J Biol Chem 2008 : We find that TRAF6 also localizes in the nuclei of osteoclasts but not their bone marrow macrophage precursors and that osteoclast intranuclear abundance is specifically increased by RANK ligand (RANKL)