Molecular mechanism of proteolytic cleavage of Reelin

Reelin是一种对大脑发育至关重要的大蛋白质。Reelin在特定位点被蛋白水解切割。本研究的目的是阐明Reelin蛋白酶解的分子机制。我们发现以下几点。(1)丝蛋白不具有蛋白水解活性。(2)具有血小板反应蛋白基序4的去整合素和金属蛋白酶（ADAMTS-4）可以以异构体依赖性方式切割Reelin。(3)具有完整CTR的Reelin与不同于众所周知的Reelin受体的跨膜蛋白结合。

Reelin is a large protein that is essential for brain development. Reelin is proteolytically cleaved at specific sites. In this study, we aimed to clarify the molecular mechanism of proteolytic cleavage of Reelin. We found following points.(1) Reelin does not have the proteolytic activity.(2) A disintegrin and metalloproteinase with thrombospondin motifs 4(ADAMTS-4) can cleave Reelin in an isoform-dependent manner.(3) Reelin with an intact CTR binds to a transmembrane protein that is different from the well-known Reelin receptors.