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首页> 外文期刊>EMBO Journal >Recruitment and activation of PLC gamma 1 in T cells: a new insight into old domains
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Recruitment and activation of PLC gamma 1 in T cells: a new insight into old domains

机译:招聘和PLCγ1 T的激活细胞:一种新的见解老域名

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摘要

Engagement of the T- cell antigen receptor leads to recruitment of phospholipase C gamma 1 ( PLC gamma 1) to the LAT- nucleated signaling complex and to PLC gamma 1 activation in a tyrosine phosphorylation- dependent manner. The mechanism of PLC gamma 1 recruitment and the role of PLC gamma 1 Src homology ( SH) domains in this process remain incompletely understood. Using a combination of biochemical methods and real- time fluorescent imaging, we show here that the N- terminal SH2 domain of PLC gamma 1 is necessary but not sufficient for its recruitment. Either the SH3 or C- terminal SH2 domain of PLC gamma 1, with the participation of Vav1, c- Cbl and Slp76, are required to stabilize PLC gamma 1 recruitment. All three PLC gamma 1 SH domains are required for phosphorylation of PLC gamma 1 Y783, which is critical for enzyme activation. These novel findings entailed revision of the currently accepted model of PLC gamma 1 recruitment and activation in T lymphocytes.
机译:订婚的T -细胞抗原受体线索γ1磷脂酶C (PLC)的招聘γ1)纬度——有核信号复杂和PLCγ1激活酪氨酸磷酸化-依赖的方式。PLCγ1招聘和PLC的角色γ1 Src同源性(SH)领域过程仍不完全清楚。结合生化方法和实时荧光成像,我们这里显示N -终端SH2 PLCγ1领域是必要的但不充分的招聘。SH3或C -末端SH2域PLCγ1,参与Vav1, c - Cbl Slp76,需要稳定PLCγ1招聘。所需的磷酸化PLCγ1 Y783,这对于酶激活是至关重要的。小说发现继承当前的修订接受的PLCγ1招聘和模式在T淋巴细胞活化。

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