Interactions of phosphatidylinositol kinase, GTPase-activating protein (GAP), and GAP-associated proteins with the colony-stimulating factor 1 receptor
Interactions of phosphatidylinositol kinase, GTPase-activating protein (GAP), and GAP-associated proteins with the colony-stimulating factor 1 receptor
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磷脂酰肌醇激酶、GTP 酶激活蛋白 (GAP) 和 GAP 相关蛋白与集落刺激因子 1 受体的相互作用
DOI：
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发表时间：
1990
影响因子：
5.3
通讯作者：
Tony PAWSONl
中科院分区：
文献类型：
--
作者：
Michael Reedijk;Xingquan Liu;Tony PAWSONl
巨噬细胞集落刺激因子1（CSF-1）受体与潜在的目标的相互作用进行了研究后，配体刺激小鼠巨噬细胞或异位表达小鼠CSF-1受体的成纤维细胞。在表达小鼠CSF-1受体的Rat-2细胞中，受体的完全活化和细胞转化需要外源性CSF-1，而表达小鼠c-fms的NIH 3 T3细胞通过自分泌刺激转化。活化的CSF-1受体与磷脂酰肌醇（PI）3 '-激酶物理结合。缺失激酶插入区的突变型CSF-1受体结合功能性PI 3 '-激酶和诱导PI 3'-激酶活性的能力不足，可与抗磷酸酪氨酸抗体沉淀。在成纤维细胞中，CSF-1刺激也诱导GTP酶激活蛋白（GAP）相关蛋白p62酪氨酸磷酸化，虽然GAP本身是一个相对较差的底物。与PI 3 '-激酶结合相反，p62和GAP的磷酸化不受激酶插入区缺失的显著影响。这些结果表明激酶插入区选择性地增强CSF-1受体与活性PI 3 ′-激酶的CSF-1依赖性结合。插入缺失突变体在NIH 3 T3细胞中保留了相当大的转化活性（G.泰勒，M。Reedijk，V. Rothwell，L. Rohrschneider和T. Pawson，EMBO J. 8：2029-2037，1989）。该突变体在Rat-2细胞转化中受损更严重，尽管在CSF-1存在下，表达突变体的Rat-2细胞仍在软琼脂中形成小集落。因此，通过CSF-1受体的活化而磷酸化GAP和p62不会导致完全的成纤维细胞转化。CSF-I受体和PI 3 '-激酶之间的相互作用可能有助于c-fms成纤维细胞转化，并在CSF-I刺激的巨噬细胞中发挥作用。
The interactions of the macrophage colony-stimulating factor 1 (CSF-1) receptor with potential targets were investigated after ligand stimulation either of mouse macrophages or of fibroblasts that ectopically express mouse CSF-1 receptors. In Rat-2 cells expressing the mouse CSF-1 receptor, full activation of the receptor and cellular transformation require exogenous CSF-1, whereas NIH 3T3 cells expressing mouse c-fms are transformed by autocrine stimulation. Activated CSF-1 receptors physically associate with a phosphatidylinositol (PI) 3'-kinase. A mutant CSF-1 receptor with a deletion of the kinase insert region was deficient in its ability to bind functional PI 3'-kinase and to induce PI 3'-kinase activity precipitable with antiphosphotyrosine antibodies. In fibroblasts, CSF-1 stimulation also induced the phosphorylation of the GTPase-activating protein (GAP)-associated protein p62 on tyrosine, although GAP itself was a relatively poor substrate. In contrast to PI 3'-kinase association, phosphorylation of p62 and GAP was not markedly affected by deletion of the kinase insert region. These results indicate that the kinase insert region selectively enhances the CSF-1-dependent association of the CSF-1 receptor with active PI 3'-kinase. The insert deletion mutant retains considerable transforming activity in NIH 3T3 cells (G. Taylor, M. Reedijk, V. Rothwell, L. Rohrschneider, and T. Pawson, EMBO J. 8:2029-2037, 1989). This mutant was more seriously impaired in Rat-2 cell transformation, although mutant-expressing Rat-2 cells still formed small colonies in soft agar in the presence of CSF-1. Therefore, phosphorylation of GAP and p62 through activation of the CSF-1 receptor does not result in full fibroblast transformation. The interaction between the CSF-1 receptor and PI 3'-kinase may contribute to c-fms fibroblast transformation and play a role in CSF-1-stimulated macrophages.
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影响因子：
56.9
作者：
M. Wahl;T. Daniel;G. Carpenter
通讯作者：
M. Wahl;T. Daniel;G. Carpenter
影响因子：
56.9
作者：
LEE, PL;JOHNSON, DE;WILLIAMS, LT
通讯作者：
WILLIAMS, LT
影响因子：
8
作者：
L. Rohrschneider;V. Rothwell;N. Nicola
通讯作者：
L. Rohrschneider;V. Rothwell;N. Nicola
表皮生长因子刺激磷脂酶 C-II 的酪氨酸磷酸化，独立于受体内化和细胞外钙。
DOI：
10.1073/pnas.86.5.1568
发表时间：
1989
影响因子：
11.1
作者：
Wahl,MI;Nishibe,S;Suh,PG;Rhee,SG;Carpenter,G
通讯作者：
Carpenter,G
影响因子：
2.7
作者：
REGENSTREIF, LJ;ROSSANT, J
通讯作者：
ROSSANT, J