Latest research on Threonine

An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins. [PubChem]

Latest findings

Several members of the Rho GTPases have been shown to be regulated by serine, Threonine or TYROSINE phosphorylation. [source, 2016]
These mutants include GFP-tagged mutant RhoA with mutation of either serine 88 or Threonine 100 to Alanine, or both sites to Alanine (GFP-RhoA S88A, GFP-RhoA T100A, and GFP-RhoA S88A/T100A), GFP-tagged mutant RhoA with mutation of either serine 88 or Threonine 100 to Glutamic acid, or both sites to Glutamic acid (GFP-RhoA S88E, GFP-RhoA T100E, and GFP-RhoA S88E/T100E). [source, 2016]
Constructs encoding GFP-tagged mutant RhoA (PBR Rac1) with the mutation of serine 88 and Threonine 100 to Glutamic acid (GFP-RhoA S88E/T100ERac1-PBR) and GFP-Rac1 T108ERhoA-PBR were generated by further mutation of 88S and 100T to E using the method described above, with GFP-Rac1RhoA-PBR and GST-RhoARac1-PBR as templates. [source, 2016]
Mutation of 88S substantially reduced the phosphorylation level of RhoA serine phosphorylation, but had no effect on the Threonine phosphorylation of RhoA. [source, 2016]
Similarly, mutation of 100T strongly inhibited RhoA Threonine phosphorylation, but had no effect on RhoA serine phosphorylation. [source, 2016]
Mutation of both 88S and 100T simultaneously inhibits EGF-induced serine and Threonine phosphorylation of RhoA. [source, 2016]
It is well documented that ERK phosphorylates the serine or Threonine in the dipeptide motif S/T-P of target substrates, and there is some preference for PROLINE at the -2 or -3 positions relative to the phosphorylated residue [27]. [source, 2016]
Phosphorylation is catalyzed by enzymes called Protein Kinases (PK) that catalyze the transfer of γ-phosphate of ATP to serine, Threonine or TYROSINE residues on target proteins. [source, 2016]
The O-linked β-N-acetylglucosamine (O-GlcNAc) modification is a monosaccharide addition that occurs in nuclear and cytoplasmic proteins such as transcription factors, cytoskeletal proteins, nuclear pore proteins, oncogenes, and tumor suppressors specifically on serine (Ser) or Threonine (Thr) residues. [source, 2016]
The uridine 5′-diphospho-N-acetylglucosamine (UDP-GlcNAc) is transferred to serine or Threonine residues by the O-GlcNAc transferase (OGT) to produce the O-GlcNAc modification, while the removal of the modification is performed by an O-GlcNAcase [134, 135]. [source, 2016]