phosphotyrosine การใช้

• PTP1B can dephosphorylate the phosphotyrosine residues of the activated insulin receptor kinase.
• Mass spectrometry is subsequently used to identify phosphoserine, phosphothreonine, and phosphotyrosine-containing peptides.
• These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine / threonine and phosphotyrosine residues.
• Mutations in the SH2 and SH3 domains that disrupt binding of phosphotyrosine lead to activation of kinase activity.
• The gene for CCM2 encodes a novel protein named malcavernin that contains a phosphotyrosine ( PTB ) binding domain.
• One family, the dual specificity phosphatases ( DSPs ) acts on both phosphotyrosine and phosphoserine / threonine residues.
• Monoclonal antibodies, from chicken embryo cells transformed by pp60v-src, recognize seven different phosphotyrosine-containing proteins.
• As their name implies, these enzymes are capable of hydrolyzing the phosphate from both phosphotyrosine and the phosphothreonine residues.
• ManLAM may also directly activate SHP-1, a phosphotyrosine phosphatase known to be involved in terminating activation signals.
• IRS-1, for example, is an IRS protein that contains a phosphotyrosine binding-domain ( motif.
• Activated tyrosine kinase receptors, on the cell surface, use proteins such as SHC1 that contain phosphotyrosine binding domains.
• This transmission is also provided by the SH2 " domain contacts responsible for the coupling of phosphotyrosine-containing proteins.
• Phosphotyrosine ( P . Tyr ) residues on activated RTKs are recognized by a phosphodependent-binding domain, the SH2 domain.
• This inactivation occurred as a result of dephosphorylation of the phosphotheronine but not the phosphotyrosine residue in the phosphorylation lip of Hog1.
• In a contrast to Src, mutations in the SH2 domain of Abl that abrogates phosphotyrosine binding do not activate Abl in vivo.
• The human topoisomerase type IB enzyme forms a covalent 3'- phosphotyrosine intermediate, the topoisomerase 1-cleavage-complex ( Top1cc ).
• Mice with truncated EpoR are viable, which suggests Jak2 activity is sufficient to support basal erythropoiesis by activating the necessary pathways without phosphotyrosine docking sites being needed.
• Thus, phosphotyrosine-dependent association of TR? with PI3K provides a potential mechanism for integrating regulation of development and metabolism by thyroid hormone and receptor tyrosine kinases.
• Numb expression was found to selectively tag the membrane Notch1 receptor for ubiquitination through the interaction of its Phosphotyrosine-binding domain with the E3 ubiquitin ligase Itch.
• Upon phosphorylation by other kinases, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation.