Comer A R, Ahern-Djamali S M, Juang J L, Jackson P D, Hoffmann F M
McArdle Laboratory for Cancer Research and Laboratory of Genetics, University of Wisconsin-Madison, 53706, USA.
Mol Cell Biol. 1998 Jan;18(1):152-60. doi: 10.1128/MCB.18.1.152.
Drosophila Enabled (Ena) is a member of a family of cytoskeleton-associated proteins including mammalian vasodilator-stimulated phosphoprotein and murine Enabled that regulate actin cytoskeleton assembly. Mutations in Drosophila ena were discovered as dominant genetic suppressors of mutations in the Abelson tyrosine kinase (Abl), suggesting that Ena and Abl function in the same pathway or process. We have identified six tyrosine residues on Ena that are phosphorylated by Abl in vitro and in vivo. Mutation of these phosphorylation sites to phenylalanine partially impaired the ability of Ena to restore viability to ena mutant animals, indicating that phosphorylation is required for optimal Ena function. Phosphorylation of Ena by Abl inhibited the binding of Ena to SH3 domains in vitro, suggesting that one effect of Ena phosphorylation may be to modulate its association with other proteins.
果蝇 Enabled（Ena）是细胞骨架相关蛋白家族的成员，该家族包括调节肌动蛋白细胞骨架组装的哺乳动物血管舒张刺激磷蛋白和小鼠 Enabled。果蝇 ena 中的突变是作为阿贝尔森酪氨酸激酶（Abl）突变的显性遗传抑制因子被发现的，这表明 Ena 和 Abl 在同一途径或过程中发挥作用。我们已经鉴定出 Ena 上六个在体外和体内被 Abl 磷酸化的酪氨酸残基。将这些磷酸化位点突变为苯丙氨酸会部分损害 Ena 恢复 ena 突变动物活力的能力，表明磷酸化是 Ena 发挥最佳功能所必需的。Abl 对 Ena 的磷酸化在体外抑制了 Ena 与 SH3 结构域的结合，这表明 Ena 磷酸化的一个作用可能是调节其与其他蛋白质的相互作用。
