HOMOLOGY OF A YEAST ACTIN-BINDING PROTEIN TO SIGNAL TRANSDUCTION PROTEINS AND MYOSIN-I
HOMOLOGY OF A YEAST ACTIN-BINDING PROTEIN TO SIGNAL TRANSDUCTION PROTEINS AND MYOSIN-I
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DOI：
10.1038/343288a0
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发表时间：
1990-01-18
期刊：
影响因子：
64.8
通讯作者：
BOTSTEIN, D
中科院分区：
文献类型：
--
作者：
DRUBIN, DG;MULHOLLAND, J;BOTSTEIN, D
在酵母中，皮质肌动蛋白细胞骨架似乎指定了细胞表面的生长部位1，2。由于肌动蛋白结合蛋白ABPlp与酿酒酵母的皮质细胞骨架有关，它可能参与细胞表面生长的空间组织3。ABPlp定位于皮质细胞骨架，其过量生产导致皮质肌动蛋白细胞骨架在细胞表面不适当的位置组装，导致非局域性表面生长。我们现在已经克隆了ABPlp的编码基因并进行了测序。ABPlp是一种新的蛋白，具有50个氨基酸残基，与非受体酪氨酸激酶(包括原癌基因c-src和c-abl编码的蛋白)非催化区的SH3结构域、磷脂酶Cγ和α-Spectrin非常相似。我们还在肌球蛋白-I的肌动蛋白结合尾部结构域中发现了一个SH3相关的基序。对与膜细胞骨架无关的蛋白家族中SH3结构域的鉴定表明，该结构域可能将膜细胞骨架中的信号转导蛋白和它们的靶标或调节器结合在一起，或两者兼而有之。
IN yeast, the cortical actin cytoskeleton seems to specify sites of growth of the cell surface1,2. Because the actin-binding protein ABPlp is associated with the cortical cytoskeleton ofSaccharomyces cerevisiae, it might be involved in the spatial organization of cell surface growth3. ABPlp is localized to the cortical cytoskeleton and its overproduction causes assembly of the cortical actin cytoskeleton at inappropriate sites on the cell surface, resulting in delocalized surface growth. We have now cloned and sequen-ced the gene encoding ABPlp. ABPlp is a novel protein with a 50 amino-acid C-terminal domain that is very similar to the SH3 domain in the non-catalytic region of nonreceptor tyrosine kinases (including those encoded by the proto-oncogenes c-srcand c-abl), in phopholipase Cγ and in α-spectrin. We also identified an SH3-related motif in the actin-binding tail domain of myosin-I. The identification of SH3 domains in a family of otherwise unrelated proteins that associate with the membrane cytoskeleton indicates that this domain might serve to bring together signal transduction proteins and their targets or regulators, or both, in the membrane cytoskeleton.