tgf beta receptor การใช้

• The TGF beta receptor-endoglin complex relay contradicting signals from TGF beta as well.
• Transforming growth factor, beta 3 has been shown to interact with TGF beta receptor 2.
• It binds to the MH2 domain of the R-SMADs SMAD2 and SMAD3 as well as the type I TGF beta receptors.
• Endoglin has been shown to TGF beta receptor 3 and TGF beta receptor 1, and with lower affinity to TGF beta receptor 2.
• Endoglin has been shown to TGF beta receptor 3 and TGF beta receptor 1, and with lower affinity to TGF beta receptor 2.
• Endoglin has been shown to TGF beta receptor 3 and TGF beta receptor 1, and with lower affinity to TGF beta receptor 2.
• Furthermore, TGF beta receptor I will dissociate from endoglin soon after it phosphorylates its cytoplasmic tail, leaving TGF beta receptor I inactive.
• Furthermore, TGF beta receptor I will dissociate from endoglin soon after it phosphorylates its cytoplasmic tail, leaving TGF beta receptor I inactive.
• SMAD3 is recruited by SARA ( SMAD Anchor for Receptor Activation ) located in the cytosolic part of the TGF beta receptors and Activin receptors.
• The full length endoglin will bind to the TGF beta receptor complex whether TGF beta is bound or not, but the truncated forms of endoglin have more specific binding.
• Endoglin itself doesn't bind the TGF beta ligands, but is present with the TGF beta receptors when the ligand is bound, indicating an important role for endoglin.
• The Argos domain has features in common with the three finger toxin fold that is found in a number of proteins including TGF beta receptors and the urokinase ( uPA ) receptor.
• Unlike TGF beta receptor I which can only bind the cytoplasmic tail when its kinase domain is inactive, TGF beta receptor II can bind endoglin with an inactive and active kinase domain.
• Unlike TGF beta receptor I which can only bind the cytoplasmic tail when its kinase domain is inactive, TGF beta receptor II can bind endoglin with an inactive and active kinase domain.
• The high interaction between endoglin's cytoplasmic and extracellular tail with the TGF beta receptor complexes indicates an important role for endoglin in the modulation of the TGF beta responses, such as cellular localization and cellular migration.
• Endoglin can also mediate F-actin dynamics, focal adhesions, microtubular structures, endocytic vesicular transport through its interaction with zyxin, ZRP-1, beta-arrestin and Tctex2beta, LK1, ALK5, TGF beta receptor II, and GIPC.
• The important role that endoglin plays in angiogenesis and the modulation of TGF beta receptor signaling, which mediates cellular localization, cellular migration, cellular morphology, cell proliferation, cluster formation, etc ., makes endoglin an important player in tumor growth and metastasis.
• The amino acid ( aa ) region 437-558 in the extracellular domain of endoglin will bind to TGF beta receptor II . TGF beta receptor I binds to the 437-588 aa region and to the aa region between 437 and the N-terminus.
• The amino acid ( aa ) region 437-558 in the extracellular domain of endoglin will bind to TGF beta receptor II . TGF beta receptor I binds to the 437-588 aa region and to the aa region between 437 and the N-terminus.
• It has been shown that the C-terminal portion of this protein is sufficient for binding and activation of TAK1, while a portion of the N-terminus acts as a dominant-negative inhibitor of TGF beta, suggesting that this protein may function as a mediator between TGF beta receptors and TAK1.