Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on merlin localization
Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on merlin localization
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DOI：
10.1074/jbc.m200083200
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发表时间：
2002-03-22
影响因子：
4.8
通讯作者：
Jacks, T
中科院分区：
文献类型：
--
作者：
Kissil, JL;Johnson, KC;Jacks, T
NF2肿瘤抑制基因产物Merlin与条带4.1超家族的膜细胞骨架接头蛋白有关，包括Ezrin，Radixin和Moesin（ERMS）。 Merlin以RAC/CDC42依赖性方式受磷酸化的调节。我们报告说，丝氨酸518上梅林的磷酸化是由P21激活的激酶PAK2诱导的。这是通过生化分馏，PAK2的主动和显性阴性突变体的使用以及免疫序列证明的。通过使用野生型和突变形式的Merlin和磷酸化指导抗体，我们表明Merlin在丝氨酸518处的磷酸化会导致巨大的蛋白质重新定位。
The Nf2 tumor suppressor gene product merlin is related to the membrane-cytoskeleton linker proteins of the band 4.1 superfamily, including ezrin, radixin, and moesin (ERMs). Merlin is regulated by phosphorylation in a Rac/cdc42-dependent fashion. We report that the phosphorylation of merlin at serine 518 is induced by the p21-activated kinase PAK2. This is demonstrated by biochemical fractionation, use of active and dominant-negative mutants of PAK2, and immunodepletion. By using wild-type and mutated forms of merlin and phospho-directed antibodies, we show that phosphorylation of merlin at serine 518 leads to dramatic protein relocalization.