Furuta Y, Ilić D, Kanazawa S, Takeda N, Yamamoto T, Aizawa S
Department of Morphogenesis, Kumamoto University School of Medicine, Japan.
Oncogene. 1995 Nov 16;11(10):1989-95.
FAK is a unique non-receptor protein tyrosine kinase that was found in cellular focal adhesions. An increasing number of in vitro observations has suggested that FAK mediates signaling through integrins brought about by interactions with extracellular matrix (ECM). It is highly tyrosine-phosphorylated in v-src-transformed cells and during embryogenesis. To clarify the function of FAK in cell-ECM interactions, embryonic phenotype of its mutant was analysed. FAK-deficient embryos could implant and initiate gastrulation normally, but showed abnormalities in subsequent development. The abnormalities were characterized as a general deficiency in mesoderm, and the phenotype was quite similar to that caused by fibronectin-deficiency. The results suggest that FAK mediates fibronectin-integrin interactions uniquely at this stage of development, thereby playing an essential role in development of mesodermal cell lineages.
粘着斑激酶（FAK）是一种独特的非受体蛋白酪氨酸激酶，发现于细胞粘着斑中。越来越多的体外观察表明，FAK通过与细胞外基质（ECM）相互作用所引发的整合素介导信号传导。它在v-src转化细胞以及胚胎发育过程中高度酪氨酸磷酸化。为阐明FAK在细胞与ECM相互作用中的功能，对其突变体的胚胎表型进行了分析。缺乏FAK的胚胎能够正常着床并启动原肠胚形成，但在随后的发育中出现异常。这些异常表现为中胚层普遍缺陷，其表型与纤连蛋白缺乏所导致的表型非常相似。结果表明，FAK在发育的这一阶段独特地介导纤连蛋白 - 整合素相互作用，从而在中胚层细胞谱系的发育中发挥重要作用。
