[HTML][HTML] A mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the α, β-hydrolase fold protein family
A De Jaco, D Comoletti, Z Kovarik, G Gaietta… - Journal of biological …, 2006 - ASBMB
A mutation linked to autistic spectrum disorders encodes an Arg to Cys replacement in the C-
terminal portion of the extracellular domain of neuroligin-3. The solvent-exposed Cys causes
virtually complete retention of the protein in the endoplasmic reticulum when the protein is
expressed in transfected cells. An identical Cys substitution was reported for
butyrylcholinesterase through genotyping patients with post-succinylcholine apnea.
Neuroligin, butyrylcholinesterase, and acetylcholinesterase are members of the α, β …
terminal portion of the extracellular domain of neuroligin-3. The solvent-exposed Cys causes
virtually complete retention of the protein in the endoplasmic reticulum when the protein is
expressed in transfected cells. An identical Cys substitution was reported for
butyrylcholinesterase through genotyping patients with post-succinylcholine apnea.
Neuroligin, butyrylcholinesterase, and acetylcholinesterase are members of the α, β …