Signal transduction by fibroblast growth factor receptors
Signal transduction by fibroblast growth factor receptors
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DOI：
10.2741/klint
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发表时间：
1999-02-15
期刊：
影响因子：
--
通讯作者：
Claesson-Welsh, Lena
中科院分区：
文献类型：
--
作者：
Klint, Peter;Claesson-Welsh, Lena
成纤维细胞生长因子家族及其原型成员酸性 FGF (FGF-1) 和碱性 FGF (FGF-2) 与四种相关受体酪氨酸激酶结合，在组织培养中的大多数类型细胞上表达。在许多方面，FGF 受体与其他生长因子受体相似。因此，配体结合后受体单体的二聚化可能是激活激酶结构域的必要条件，从而导致受体反式磷酸化。 FGF 受体-1 (FGFR-1) 显示四种 FGF 受体中最广泛的表达模式，包含至少七个酪氨酸磷酸化位点。许多信号转导分子因与这些磷酸化位点的不同亲和力结合而受到影响。讨论了这些信号转导分子在 FGF 诱导的生物反应和病理过程中的潜在作用。
The fibroblast growth factor family, with its prototype members acidic FGF (FGF-1) and basic FGF (FGF-2), binds to four related receptor tyrosine kinases, expressed on most types of cells in tissue culture. In many respects, the FGF receptors appear similar to other growth factor receptors. Thus, dimerization of receptor monomers upon ligand binding is likely to be a requisite for activation of the kinase domains, leading to receptor trans phosphorylation. FGF receptor-1 (FGFR-1), which shows the broadest expression pattern of the four FGF receptors contains at least seven tyrosine phosphorylation sites. A number of signal transduction molecules are affected by binding with different affinities to these phosphorylation sites. The potential roles of these signal transduction molecules in FGF-induced biological responses and in pathological processes are discussed.