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2018 ; 34
(5
): 721-724
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gab.com Text
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TMEM132: an ancient architecture of cohesin and immunoglobulin domains define a
new family of neural adhesion molecules
#MMPMID29088312
Sanchez-Pulido L
; Ponting CP
Bioinformatics
2018[Mar]; 34
(5
): 721-724
PMID29088312
show ga
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.