泛素与一部分SH3结构域结合并对其进行调节。
Ubiquitin binds to and regulates a subset of SH3 domains.
作者信息
Stamenova Svetoslava D, French Michael E, He Yuan, Francis Smitha A, Kramer Zachary B, Hicke Linda
机构信息
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
出版信息
Mol Cell. 2007 Jan 26;25(2):273-84. doi: 10.1016/j.molcel.2006.12.016.
SH3 domains are modules of 50-70 amino acids that promote interactions among proteins, often participating in the assembly of large dynamic complexes. These domains bind to peptide ligands, which usually contain a core Pro-X-X-Pro (PXXP) sequence. Here we identify a class of SH3 domains that bind to ubiquitin. The yeast endocytic protein Sla1, as well as the mammalian proteins CIN85 and amphiphysin, carry ubiquitin-binding SH3 domains. Ubiquitin and peptide ligands bind to the same hydrophobic groove on the SH3 domain surface, and ubiquitin and a PXXP-containing protein fragment compete for binding to SH3 domains. We conclude that a subset of SH3 domains constitutes a distinct type of ubiquitin-binding domain and that ubiquitin binding can negatively regulate interaction of SH3 domains with canonical proline-rich ligands.
SH3结构域是由50 - 70个氨基酸组成的模块，可促进蛋白质之间的相互作用，常参与大型动态复合物的组装。这些结构域与肽配体结合，肽配体通常包含核心序列Pro-X-X-Pro（PXXP）。在此，我们鉴定出一类与泛素结合的SH3结构域。酵母内吞蛋白Sla1以及哺乳动物蛋白CIN85和发动蛋白均带有泛素结合SH3结构域。泛素和肽配体结合在SH3结构域表面的同一疏水凹槽上，泛素和含PXXP的蛋白质片段竞争与SH3结构域的结合。我们得出结论，一部分SH3结构域构成了一种独特类型的泛素结合结构域，并且泛素结合可负向调节SH3结构域与典型富含脯氨酸配体的相互作用。
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