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首页> 外文期刊>Molecular and Cellular Biology >A Novel and Conserved Protein-Protein Interaction Domain of Mammalian Lin-2/CASK Binds and Recruits SAP97 to the Lateral Surface of Epithelia
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A Novel and Conserved Protein-Protein Interaction Domain of Mammalian Lin-2/CASK Binds and Recruits SAP97 to the Lateral Surface of Epithelia

机译：哺乳动物Lin-2 / CASK的新型和保守的蛋白质-蛋白质相互作用域绑定并招募SAP97到上皮细胞的侧表面

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Mammalian Lin-2 (mLin-2)/CASK is a membrane-associated guanylate kinase (MAGUK) and contains multidomain modules that mediate protein-protein interactions important for the establishment and maintenance of neuronal and epithelial cell polarization. The importance of mLin-2/CASK in mammalian development is demonstrated by the fact that mutations in mLin-2/CASK or SAP97, another MAGUK protein, lead to cleft palate in mice. We recently identified a new protein-protein interaction domain, called the L27 domain, which is present twice in mLin-2/CASK. In this report, we further define the binding of the L27C domain of mLin-2/CASK to the L27 domain of mLin-7 and identify the binding partner for L27N of mLin-2/CASK. Biochemical analysis reveals that this L27N domain binds to the N terminus of SAP97, a region that was previously reported to be essential for the lateral membrane recruitment of SAP97 in epithelia. Our colocalization studies, using dominant-negative mLin-2/CASK, show that the association with mLin-2/CASK is crucial for lateral localization of SAP97 in MDCK cells. We also report the identification of a novel isoform of Discs Large, a Drosophila melanogaster orthologue of SAP97, which contains a region highly related to the SAP97 N terminus and which binds Camguk, a Drosophila orthologue of mLin-2/CASK. Our data identify evolutionarily conserved protein-protein interaction domains that link mLin-2/CASK to SAP97 and account for their common phenotype when mutated in mice.
机译：哺乳动物Lin-2（mLin-2）/ CASK是膜相关的鸟苷酸激酶（MAGUK），并包含介导蛋白-蛋白相互作用的多域模块，这些相互作用对于建立和维持神经元和上皮细胞极化非常重要。 mLin-2 / CASK或另一种MAGUK蛋白的SAP97突变导致小鼠mutation裂的事实证明了mLin-2 / CASK在哺乳动物发育中的重要性。我们最近确定了一个新的蛋白质-蛋白质相互作用域，称为L27域，该域在mLin-2 / CASK中存在两次。在本报告中，我们进一步定义了mLin-2 / CASK的L27C结构域与mLin-7的L27结构域的结合，并确定了mLin-2 / CASK的L27N的结合伴侣。生化分析表明，该L27N结构域与SAP97的N末端结合，该区域先前据报道对于SAP97在上皮细胞的侧膜募集至关重要。我们使用显性阴性mLin-2 / CASK进行的共定位研究表明，与mLin-2 / CASK的关联对于SAPCK在MDCK细胞中的侧向定位至关重要。我们还报告了对Discs Large的新型同种型的鉴定，这是SAP97的果蝇直角同源物，其中包含与SAP97 N末端高度相关的区域，并与Camguk结合， mLin-2 / CASK的果蝇直系同源物。我们的数据确定了将mLin-2 / CASK连接到SAP97的进化保守蛋白-蛋白相互作用域，并解释了它们在小鼠中发生突变时的共同表型。

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