
癌症免疫治疗相关的TCR信号通路研究新进展 - 知乎
LCK激酶活性受两种关键调节性酪氨酸Y394和Y505的磷酸化和去磷酸化控制(图五)。 Y394位于LCK激酶环中,自磷酸化可以稳定催化结构域的活性构象。
细胞免疫研究的核心通路——T cell receptor signaling pathway( …
2022年7月11日 · 酪氨酸激酶LCK是TCR通路的一个关键调节结点,LCK的构象以及细胞定位变化将影响TCR信号传导。 LCK的活性调节受其两个酪氨酸残基磷酸化的影响:位于催化结构域活化环的Y394位点磷酸化对LCK活性是正调节,而位于羧基末端的Y505位点的磷酸化则对蛋白活性有负 …
Biophysical basis underlying dynamic Lck activation visualized by ...
While modifications of K287 and Y505 have been shown to have activating and inhibitory effects on Lck activity, respectively, the role of Y394 remains unclear. Phosphorylation of Y394 has been suggested to stabilize the open active conformation of Lck and positively contribute to Lck kinase activation, and the tyrosine-to-phenylalanine mutation ...
Bound to be perfect: Lck and T cell co-receptors - Nature
2023年1月3日 · Phosphorylation of Tyr505 (Y505) of Lck enables the C terminus to bind to the SH2 domain, keeping Lck in an inactive conformation. When Tyr505 is dephosphorylated...
Encoding optical control in LCK kinase to quantitatively investigate ...
2017年10月30日 · Previous studies have shown that the SH2 domain of LCK can bind intramolecularly to a phosphorylated residue (Y505) at the C terminus to adopt a closed autoinhibitory conformation, which is a...
Inhibiting ACK1-mediated phosphorylation of C-terminal Src …
2022年11月14日 · LCK Y394 phosphorylation in the activation loop is needed to acquire full kinase activity; in contrast, Y505 phosphorylation in the C-terminal tail, which interacts with its own SH2 domain and...
Tyrosine 192 within the SH2 domain of the Src-protein tyrosine …
2020年11月23日 · The enzymatic activity of Lck is primarily regulated via reversible and dynamic phosphorylation of two tyrosine residues, Y394 and Y505. Lck possesses an additional highly conserved tyrosine Y192, located within the SH2 domain, whose role in T-cell activation is not fully understood.
Molecular Cell(回顾)|Lck的磷酸化位点调节CD45对Lck的激活 …
2020年6月21日 · Lck是SFK家族激酶的一种,其活性主要由SH2和SH3结构域及两个酪氨酸磷酸化位点Y505和Y394调节(Fig 1A)。 调控结构域中的磷酸化对Lck的构象,进而对其活性有调控作用(Fig 1B)。
Expression of the p56lck Y505F Mutation in CD45-Deficient Mice …
To determine whether the block in thymocyte development was due to the inability to dephosphorylate the inhibitory phosphorylation site (Y505) in p56 lck (Lck), we generated CD45-deficient mice that express transgenes for the Lck Y505F mutation and the DO11.10 T-cell antigen receptor (TCR).
Lck bound to coreceptor is less active than free Lck | PNAS
2020年6月22日 · Lck activity is tightly regulated by the phosphorylation and dephosphorylation of the activating tyrosine 394 (Y394) and the inhibitory Y505 (11). The Y505 of Lck can be phosphorylated by C-terminal Src kinase (Csk), resulting in a closed conformation with inhibited kinase activity (11).