p59fyn tyrosine kinase associates with multiple T-cell receptor subunits through its unique amino-terminal domain
p59fyn tyrosine kinase associates with multiple T-cell receptor subunits through its unique amino-terminal domain
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p59fyn 酪氨酸激酶通过其独特的氨基末端结构域与多个 T 细胞受体亚基相关
DOI：
10.1128/mcb.12.12.5438-5446.1992
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发表时间：
1992
影响因子：
5.3
通讯作者：
Andrey S. Shaw
中科院分区：
文献类型：
--
作者：
Lisa K. Timson;Gauen;A.;Kong;E. Lawrence;Samelson;Andrey S. Shaw
Several lines of evidence link the protein tyrosine kinase p59fyn to the T-cell receptor. The molecular basis of this interaction has not been established. Here we show that the tyrosine kinase p59fyn can associate with chimeric proteins that contain the cytoplasmic domains of CD3 epsilon, gamma, zeta (zeta), and eta. Mutational analysis of the zeta cytoplasmic domain demonstrated that the membrane-proximal 41 residues of zeta are sufficient for p59fyn binding and that at least two p59fyn binding domains are present. The association of p59fyn with the zeta chain was specific, as two closely related Src family protein tyrosine kinases, p60src and p56lck, did not associate with a chimeric protein that contained the cytoplasmic domain of zeta. Mutational analysis of p59fyn revealed that a 10-amino-acid sequence in the unique amino-terminal domain of p59fyn was responsible for the association with zeta. These findings support evidence that p59fyn is functionally and structurally linked to the T-cell receptor. More importantly, these studies support a critical role for the unique amino-terminal domains of Src family kinases in the coupling of tyrosine kinases to the signalling pathways of cell surface receptors.
影响因子：
14.9
作者：
HEMSLEY, A;ARNHEIM, N;GALAS, DJ
通讯作者：
GALAS, DJ
影响因子：
11.4
作者：
JACKSON, MR;NILSSON, T;PETERSON, PA
通讯作者：
PETERSON, PA
鉴定 NADH-细胞色素 b5 还原酶的 NH2 末端封闭基团为肉豆蔻酸，以及膜结合域的完整氨基酸序列。
DOI：
--
发表时间：
1984
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ozols,J;Carr,SA;Strittmatter,P
通讯作者：
Strittmatter,P