van Slegtenhorst M, Nellist M, Nagelkerken B, Cheadle J, Snell R, van den Ouweland A, Reuser A, Sampson J, Halley D, van der Sluijs P
MGC Department of Clinical Genetics, Erasmus University, 3015GE Rotterdam, The Netherlands.
Hum Mol Genet. 1998 Jun;7(6):1053-7. doi: 10.1093/hmg/7.6.1053.
Tuberous sclerosis (TSC) is an autosomal dominant disorder caused by a mutation in either the TSC1 or TSC2 tumour suppressor gene. The disease is characterized by a broad phenotypic spectrum that can include seizures, mental retardation, renal dysfunction and dermatological abnormalities. TSC2 encodes tuberin, a putative GTPase activating protein for rap1 and rab5. The TSC1 gene was recently identified and codes for hamartin, a novel protein with no significant homology to tuberin or any other known vertebrate protein. Here, we show that hamartin and tuberin associate physically in vivo and that the interaction is mediated by predicted coiled-coil domains. Our data suggest that hamartin and tuberin function in the same complex rather than in separate pathways.
结节性硬化症（TSC）是一种常染色体显性疾病，由TSC1或TSC2肿瘤抑制基因的突变引起。该疾病具有广泛的表型谱，可包括癫痫发作、智力迟钝、肾功能障碍和皮肤异常。TSC2编码结节蛋白，一种推测的rap1和rab5的GTP酶激活蛋白。TSC1基因最近被鉴定出来，编码错构瘤蛋白，一种与结节蛋白或任何其他已知脊椎动物蛋白无显著同源性的新型蛋白。在这里，我们表明错构瘤蛋白和结节蛋白在体内发生物理结合，并且这种相互作用是由预测的卷曲螺旋结构域介导的。我们的数据表明，错构瘤蛋白和结节蛋白在同一复合物中发挥作用，而不是在单独的途径中。
