Identification of erythrocyte p55/MPP1 as a binding partner of NF2 tumor suppressor protein/Merlin.
Identification of erythrocyte p55/MPP1 as a binding partner of NF2 tumor suppressor protein/Merlin.
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DOI：
10.3181/0809-rm-275
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发表时间：
2009-03
期刊：
影响因子：
--
通讯作者：
Chishti AH
中科院分区：
文献类型：
--
作者：
Seo PS;Quinn BJ;Khan AA;Zeng L;Takoudis CG;Hanada T;Bolis A;Bolino A;Chishti AH
2型神经纤维瘤病是一种遗传性疾病，其特征在于听觉神经和中枢神经系统上的良性和恶性肿瘤的发展，症状包括听力损失、平衡不良、皮肤病变和白内障。在这里，我们报告了一种新的蛋白质-蛋白质之间的相互作用NF 2蛋白（梅林或Schwannomin）和红细胞p55，也指定为MPP 1。p55是一种保守的支架蛋白，在视网膜的细胞形状、毛细胞发育和神经模式中具有假定的功能。NF 2蛋白的FERM结构域直接与p55结合，表面等离子体共振分析表明具有3.7 nM kD值的特异性相互作用。我们开发了一种针对人红细胞p55的特异性单克隆抗体，并发现p55和NF 2蛋白在非髓鞘形成的雪旺细胞中共定位。这一发现表明，p55-NF 2蛋白的相互作用可能在非红系细胞的顶基底极性和肿瘤抑制途径的调节中发挥功能性作用。
Neurofibromatosis type 2 is an inherited disorder characterized by the development of benign and malignant tumors on the auditory nerves and central nervous system with symptoms including hearing loss, poor balance, skin lesions, and cataracts. Here, we report a novel protein-protein interaction between NF2 protein (merlin or schwannomin) and erythrocyte p55, also designated as MPP1. The p55 is a conserved scaffolding protein with postulated functions in cell shape, hair cell development, and neural patterning of the retina. The FERM domain of NF2 protein binds directly to p55, and surface plasmon resonance analysis indicates a specific interaction with a kD value of 3.7 nM. We developed a specific monoclonal antibody against human erythrocyte p55, and found that both p55 and NF2 proteins are colocalized in the non-myelin-forming Schwann cells. This finding suggests that the p55-NF2 protein interaction may play a functional role in the regulation of apicobasal polarity and tumor suppression pathways in non-erythroid cells.