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SMAD SXS Phosphorylation    

TGF-beta signaling regulates cell proliferation, differentiation, adhesion and migration in embryonic and adult tissues. The TGF-beta superfamily encompasses a large group of structurally related extracellular ligand proteins, which include TGFB1 and BMP-2. TGF-beta receptors dimerize and phosphorylate various effector proteins, including the SMAD transcription factors. Upon cellular stimulation by TGF-beta ligands, SMAD proteins assemble into multimeric complexes, which then translocate to the nucleus to regulate the expression of several hundred target genes. SXS phosphorylation also uncouples R-SMAD from cytoplasmic anchors and promotes interactions with nuclear import factors. SignalChem manufactures a wide range of recombinant SMAD proteins and Active TGF-beta receptors.

Activation of R-SMAD through SXS phosphorylation

Methylation is involved in regulating many aspects of cell function. Methyltransferases are enzymes that transfer methyl groups onto substrates. Demethylases and protein methyl esterases are responsible for reversing the modification.

The serine/threonine phosphatase PP2A holoenzyme is activated by methylation of the catalytic subunit (PP2Ac). The addition and removal of methyl groups on PP2A are catalyzed LCMT1 and PPME1, respectively.

Active PP2A dephosphorylates targets such as Tau and several serine/threonine kinases (STKs), many of which are implicated in oncogenesis. Loss of LCMT1 function can lead to an excess of phosphorylated proteins. In the brain, abundance of hyperphosphorylated Tau precipitate to form neurofibrillary tangles, the primary markers for Alzheimer’s Disease.
PP2A Regulation by LCMT1/PPME1. A: Structural Subunit, B: Regulatory Subunit, C: Catalytic Subunit
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