Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
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DOI：
10.1074/jbc.m111.270751
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发表时间：
2011-12-16
影响因子：
4.8
通讯作者：
Lu, Xin
中科院分区：
文献类型：
--
作者：
Llanos, Susana;Royer, Christophe;Lu, Xin
背景：调节亚基赋予蛋白磷酸酶底物特异性。结果：与ASPP2不同，iASPP通过其SH3结构域内的非规范结合基序与蛋白磷酸酶1 （PP1）相互作用。结论：iASPP是一种新的pp1结合伙伴。意义：所有ASPP家族成员作为PP1结合伙伴的鉴定扩展了我们对PP1活性如何在体内调节的理解。
Background: Regulatory subunits confer substrate specificity to protein phosphatases.Results: iASPP, unlike ASPP2, interacts with protein phosphatase 1 (PP1) via a noncanonical binding motif within its SH3 domain.Conclusion: iASPP is a new PP1-binding partner.Significance: The identification of all ASPP family members as PP1-binding partners extends our understanding of how PP1 activity may be regulated in vivo.