A novel transglutaminase activator forms a complex with type 1 transglutaminase
A novel transglutaminase activator forms a complex with type 1 transglutaminase
复制标题
DOI：
10.1038/sj.onc.1208392
复制
发表时间：
2005-04-21
期刊：
影响因子：
8
通讯作者：
Eckert, RL
中科院分区：
文献类型：
--
作者：
Sturniolo, MT;Chandraratna, RAS;Eckert, RL
I型转氨酶是质膜锚定的细胞内蛋白质-蛋白质交联酶，其负责在终末角质形成细胞分化期间角质形成细胞皮质包膜的组装。我们最近描述了一种新的蛋白质，TIG 3，当在角质形成细胞中表达时，会导致转氨酶活性增加和角质形成细胞死亡。然而，TIG 3激活转氨酶的机制尚不清楚。我们现在扩展了我们以前的研究，并表明全长TIG 3与I型转氨酶形成复合物，这通过TIG 3-转氨酶共沉淀来证明。我们还表明，治疗TIG 3表达细胞与单丹酰尸胺，竞争性转氨酶底物，减弱TIG 3依赖性反应，表明转氨酶是一个重要的调解人的TIG 3行动。这些发现表明，TIG 3与转氨酶形成复合物，导致转氨酶活化，并且转氨酶活性是TIG 3依赖性生物应答所需的。
Type I transglutaminase is a plasma membrane-anchored intracellular protein-protein crosslinking enzyme that is responsible for assembly of the keratinocyte cornified envelope during terminal keratinocyte differentiation. We recently described a novel protein, TIG3, that when expressed in keratinocytes causes increased transglutaminase activity and keratinocyte cell death. However, the mechanism of activation of transglutaminase by TIG3 is not known. W e now extend our previous study and show that full-length TIG3 forms a complex with type I transglutaminase that is demonstrated by TIG3-transglutaminase co-precipitation. We also demonstrate that treating TIG3-expressing cells with monodansyl cadaverine, a competitive transglutaminase substrate, attenuates the TIG3-dependent response, suggesting that transglutaminase is an important mediator of TIG3 action. These findings suggest that TIG3 forms a complex with transglutaminase resulting in transglutaminase activation and that transglutaminase activity is required for the TIG3-dependent biological response.