FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity complex
FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity complex
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DOI：
10.1016/j.yexcr.2007.08.025
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发表时间：
2007-11-15
影响因子：
3.7
通讯作者：
Roepman, Ronald
中科院分区：
文献类型：
--
作者：
Gosens, Ilse;Sessa, Alessandro;Roepman, Ronald
细胞极性是通过特殊的细胞-细胞连接将顶侧和基底侧区域分离来诱导和维持的。Crumbs蛋白及其结合伴侣参与粘附连接的形成和稳定。在这项研究中，我们描述了一种新的组成部分的哺乳动物Crumbs复杂的FERM结构域蛋白EPB 41 L5，它与所有三个Crumbs同源物的细胞内结构域通过其FERM结构域。令人惊讶的是，相同的FERM结构域参与结合MPP 5/PALS 1的HOOK结构域，这是先前鉴定的Crumbs相互作用物。共表达和共定位研究表明，在几个上皮衍生的组织中，Epb4.1l5与至少一个Crumbs同源物和Mpp 5相互作用。虽然在早期胚胎阶段发现Epb4.1l5在基底外侧膜室，在成人组织中，它共定位在顶端域与Crumbs蛋白和Mpp 5。Epb4.1l5在极化MDCK细胞中的过表达影响细胞连接的紧密性，并导致紧密连接标志物ZO-1和PATJ的解体。我们的研究结果强调了在哺乳动物中保守的Crumbs-MPP 5-EPB 41 L5极性复合物的重要性。(C)2007年爱思唯尔公司All rights reserved.
Cell polarity is induced and maintained by separation of the apical and basolateral domains through specialized cell-cell junctions. The Crumbs protein and its binding partners are involved in formation and stabilization of adherens junctions. In this study, we describe a novel component of the mammalian Crumbs complex, the FERM domain protein EPB41L5, which associates with the intracellular domains of all three Crumbs homologs through its FERM domain. Surprisingly, the same FERM domain is involved in binding to the HOOK domain of MPP5/PALS1, a previously identified interactor of Crumbs. Co-expression and co-localization studies suggested that in several epithelial derived tissues Epb4.1l5 interacts with at least one Crumbs homolog, and with Mpp5. Although at early embryonic stages Epb4.1l5 is found at the basolateral membrane compartment, in adult tissues it co-localizes at the apical domain with Crumbs proteins and Mpp5. Overexpression of Epb4.1l5 in polarized MDCK cells affects tightness of cell junctions and results in disorganization of the tight junction markers ZO-1 and PATJ. Our results emphasize the importance of a conserved Crumbs-MPP5-EPB41L5 polarity complex in mammals. (C) 2007 Elsevier Inc. All rights reserved.