TMEM132：由黏连蛋白和免疫球蛋白结构域构成的古老结构定义了一个新的神经黏附分子家族。
TMEM132: an ancient architecture of cohesin and immunoglobulin domains define a new family of neural adhesion molecules.
机构信息
Medical Research Council Human Genetics Unit, IGMM, University of Edinburgh, Edinburgh EH4 2XU, UK.
出版信息
Bioinformatics. 2018 Mar 1;34(5):721-724. doi: 10.1093/bioinformatics/btx689.
SUMMARY
The molecular functions of TMEM132 genes remain poorly understood and under-investigated despite their mutations associated with non-syndromic hearing loss, panic disorder and cancer. Here we show the full domain architecture of human TMEM132 family proteins solved using in-depth sequence and structural analysis. We reveal them to be five previously unappreciated cell adhesion molecules whose domain architecture has an early holozoan origin prior to the emergence of choanoflagellates and metazoa. The extra-cellular portions of TMEM132 proteins contain five conserved domains including three tandem immunoglobulin domains, and a cohesin domain homologue, the first such domain found in animals. These findings strongly predict a cellular adhesion function for TMEM132 family, connecting the extracellular medium with the intracellular actin cytoskeleton.
CONTACT
luis.sanchez-pulido@igmm.ed.ac.uk.
SUPPLEMENTARY INFORMATION
Supplementary data are available at Bioinformatics online.
摘要
尽管 TMEM132 基因的突变与非综合征性听力损失、恐慌症和癌症有关，但它们的分子功能仍知之甚少，研究也不充分。本文使用深入的序列和结构分析，展示了人类 TMEM132 家族蛋白的完整结构域结构。结果表明，TMEM132 蛋白是五个以前未被识别的细胞粘附分子，其结构域结构起源于早原生物，早于领鞭毛虫和后生动物出现之前。TMEM132 蛋白的细胞外部分包含五个保守结构域，包括三个串联免疫球蛋白结构域和一个黏连蛋白同源结构域，这是在动物中发现的第一个此类结构域。这些发现强烈预测了 TMEM132 家族的细胞粘附功能，将细胞外介质与细胞内肌动蛋白细胞骨架连接起来。
联系方式：luis.sanchez-pulido@igmm.ed.ac.uk
补充信息：补充信息可在“Bioinformatics”在线获取。
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