Protein phosphatase 1alpha associates with protein tyrosine phosphatase-PEST inducing dephosphorylation of phospho-serine 39.
Protein phosphatase 1alpha associates with protein tyrosine phosphatase-PEST inducing dephosphorylation of phospho-serine 39.
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蛋白磷酸酶 1α 与蛋白酪氨酸磷酸酶 -PEST 结合，诱导磷酸丝氨酸 39 去磷酸化。
DOI：
10.1093/jb/mvp191
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发表时间：
2010
影响因子：
2.7
通讯作者：
K. Mashima
中科院分区：
文献类型：
--
作者：
Kana Nakamura;Helen E F Palmer;T. Ozawa;K. Mashima
蛋白酪氨酸磷酸酶(PTP)-PEST在多种细胞类型中表达，是细胞粘附、扩散和迁移的有效调节剂。PTP-PEST相关分子对阐明PTP-PEST的功能具有重要意义。本文中，我们确定了蛋白磷酸酶1alpha （PP1alpha）作为一种新的PTP-PEST结合蛋白，然后我们旨在确定PP1alpha如何参与PTP-PEST的Ser39位点磷酸化，其磷酸化抑制PTP-PEST的酶活性。用TPA刺激过表达外源PTP-PEST的HEK 293细胞，用抗磷酸化Ser39 PTP-PEST特异性抗体（anti-pS39-PEST Ab）评估PTP-PEST在Ser39位点的磷酸化情况。结果表明，抗ps39 - pest Ab检测到的Ser39位点磷酸化依赖于TPA处理，PTP- pest的PTP活性与抗ps39 - pest Ab免疫反应带强度呈显著负相关。共转染编码野生型PP1alpha的质粒可抑制Ser39的磷酸化，但对显性阴性PP1alpha突变体无抑制作用。此外，tpa诱导的PTP-PEST催化结构域磷酸化可以发生，但PTP-PEST催化结构域的磷酸化不能通过共转染表达野生型PP1alpha的质粒来消除。综上所述，PP1alpha与PTP- pest的非催化结构域结合，并通过磷酸化ser39来调节PTP的活性。
Protein tyrosine phosphatase (PTP)-PEST is expressed in a wide variety of several cell types and is an efficient regulator of cell adhesion, spreading and migration. PTP-PEST-associating molecules are important in elucidating the function of PTP-PEST. Herein, we have identified protein phosphatase 1alpha (PP1alpha) as a novel PTP-PEST binding protein, and then we aimed to determine how PP1alpha contributes to the phosphorylation at Ser39 of PTP-PEST, whose phosphorylation suppresses PTP-PEST enzymatic activity. The HEK 293 cells overexpressing exogenous PTP-PEST were stimulated by 12-O-tetradecanoylphorbol 13-acetate (TPA) and the phosphorylation of PTP-PEST at Ser39 was evaluated using an anti-phospho-Ser39 PTP-PEST specific antibody (anti-pS39-PEST Ab). It was demonstrated that the phosphorylation at Ser39 detected by anti-pS39-PEST Ab was dependent on TPA treatment and a significant inverse correlation between the PTP activity of PTP-PEST and anti-pS39-PEST Ab-immunoreactive band intensity. The phosphorylation of Ser39 was suppressed by co-transfection of a plasmid encoding wild-type PP1alpha, but not by that of the dominant-negative PP1alpha mutant. Furthermore, TPA-induced phosphorylation could take place in PTP-PEST catalytic domain, but the phosphorylation of PTP-PEST catalytic domain could not be abrogated by co-transfection of a plasmid expressing wild-type PP1alpha. In conclusion, PP1alpha associates with the non-catalytic domain of PTP-PEST and regulates PTP activity via dephosphorylation of phospho-Ser39.
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影响因子：
16
作者：
Cong, F;Spencer, S;Goff, SP
通讯作者：
Goff, SP
DOI：
10.1152/ajpcell.00503.2006
发表时间：
2007-06
期刊：
American journal of physiology. Cell physiology
影响因子：
--
作者：
S. Sahu;S. Núñez;Guang Bai;Anandarup Gupta
通讯作者：
S. Sahu;S. Núñez;Guang Bai;Anandarup Gupta
影响因子：
4
作者：
P. Cohen
通讯作者：
P. Cohen
DOI：
10.1016/s1357-2725(01)00154-6
发表时间：
2002-07-01
影响因子：
4
作者：
Brown, MC;Turner, CE
通讯作者：
Turner, CE