Paper Info
Title
TMEM132: an ancient architecture of cohesin and immunoglobulin domains define a new family of neural adhesion molecules.
Abstract
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.
Year
DOI
Venue
2018
10.1093/bioinformatics/btx689
BIOINFORMATICS
Field
DocType
Volume
Immunoglobulin domain,Architecture domain,Cell adhesion molecule,Protein domain,Cohesin domain,Biology,Cell adhesion,Actin,Cohesin,Bioinformatics,Computational biology,Genetics
Journal
34
Issue
ISSN
Citations 
5
1367-4803
0
PageRank 
References 
Authors
0.34
3
2
Name
Order
Citations
PageRank
Luis Sánchez-Pulido123.16
Chris P. Ponting2733283.28