The SH3 domain of p56lck is involved in binding to phosphatidylinositol 3'-kinase from T lymphocytes
The SH3 domain of p56lck is involved in binding to phosphatidylinositol 3'-kinase from T lymphocytes
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p56lck 的 SH3 结构域参与与 T 淋巴细胞中的磷脂酰肌醇 3-激酶的结合
DOI：
--
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发表时间：
1993
影响因子：
5.3
通讯作者：
D. Fujita
中科院分区：
文献类型：
--
作者：
L. Vogel;D. Fujita
许多类似于Src的酪氨酸激酶被认为参与了多蛋白复合体，这些复合体通过酪氨酸磷酸化来调节跨膜信号。我们利用细菌表达的谷胱甘肽S-转移酶-p56lck融合蛋白和细胞提取物进行了体外结合研究，定位了p56lck上与磷脂酰肌醇3‘-激酶(PI3K)结合的区域。P56lck SH3结构域的缺失取消了与T细胞裂解产物的PI3K活性的结合，而SH2结构域的缺失仅导致与p56lck序列结合的PI3K活性水平的轻微下降。抗磷酸酪氨酸抗体不能阻断T细胞提取液中PI3K与p56lck的结合，但p56lck结合的PI3K活性对磷酸酶处理敏感。P56lck的SH3结构域也结合了未感染的鸡胚成纤维细胞的大部分PI3K活性。然而，用Rous肉瘤病毒v-src转化细胞的提取物观察到截然不同的结合特异性，其中大部分PI3K活性以磷酸酪氨酸依赖的方式结合到p56lck的SH2结构域。这些结果表明，PI3K与p56lck结合有两种模式，并可能与其他类似于Src的酪氨酸激酶结合。在一种模式下，来自T细胞或未感染的鸡胚胎成纤维细胞的PI3K主要与p56lck的SH3结构域结合。在另一种模式中，包括来自Rous肉瘤病毒转化细胞的PI3K，结合在很大程度上依赖于磷酸酪氨酸，并且需要p56lck的SH2结构域。
Many of the Src-like tyrosine kinases are thought to participate in multiprotein complexes that modulate transmembrane signalling through tyrosine phosphorylation. We have used in vitro binding studies employing bacterially expressed glutathione S-transferase-p56lck fusion proteins and cell extracts to map regions on p56lck that are involved in binding to phosphatidylinositol 3'-kinase (PI3K). Deletions within the SH3 domain of p56lck abolished binding of PI3K activity from T-cell lysates, whereas deletion of the SH2 domain caused only a slight reduction in the level of PI3K activity bound to p56lck sequences. The binding of PI3K from T-cell extracts to p56lck was not blocked by antiphosphotyrosine antibodies, but p56lck-bound PI3K activity was sensitive to phosphatase treatment. The SH3 domain of p56lck also bound the majority of PI3K activity from uninfected chicken embryo fibroblasts. However, a drastically different binding specificity was observed with use of extracts of Rous sarcoma virus v-src-transformed cells, in which the majority of PI3K activity bound to the SH2 domain of p56lck in a phosphotyrosine-dependent manner. These results suggest that are two modes of PI3K binding to p56lck, and presumably to other Src-like tyrosine kinases. In one mode, PI3K from T cells or uninfected chicken embryo fibroblasts binds predominantly to the SH3 domain of p56lck. In the other mode, involving PI3K from Rous sarcoma virus-transformed cells, binding is largely phosphotyrosine dependent and requires the SH2 domain of p56lck.
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DOI：
10.1073/pnas.87.10.3816
发表时间：
1990-05-01
影响因子：
11.1
作者：
BJORGE, JD;CHAN, TO;FUJITA, DJ
通讯作者：
FUJITA, DJ
CD4 和 CD8 是否通过特定的酪氨酸蛋白激酶控制 T 细胞激活？
DOI：
10.1016/0167-5699(89)90322-8
发表时间：
1989
期刊：
Immunology today
影响因子：
--
作者：
Mustelin,T;Altman,A
通讯作者：
Altman,A
CD-3 介导的 MAP-2 激酶激活可通过连接 CD4 受体进行修饰。
DOI：
--
发表时间：
1990
期刊：
Journal of immunology (Baltimore, Md. : 1950)
影响因子：
--
作者：
Nel,AE;Pollack,S;Landreth,G;Ledbetter,JA;Hultin,L;Williams,K;Katz,R;Akerley,B
通讯作者：
Akerley,B
I 型磷脂酰肌醇激酶活性与多种癌基因产物相关。
DOI：
--
发表时间：
1989
期刊：
Oncogene research
影响因子：
--
作者：
Fukui,Y;Kornbluth,S;Jong,SM;Wang,LH;Hanafusa,H
通讯作者：
Hanafusa,H