AUTHOR=Chen Vicky P., Luk Wilson K., Chan Wallace K., Leung K. Wing , Guo Ava J., Chan Gallant K., Xu Sherry L., Choi Roy C., Tsim Karl W.

TITLE=Molecular Assembly and Biosynthesis of Acetylcholinesterase in Brain and Muscle: the Roles of t-peptide, FHB Domain, and N-linked Glycosylation

JOURNAL=Frontiers in Molecular Neuroscience

VOLUME=4

YEAR=2011

URL=https://www.frontiersin.org/journals/molecular-neuroscience/articles/10.3389/fnmol.2011.00036

DOI=10.3389/fnmol.2011.00036

ISSN=1662-5099

ABSTRACT=<p>Acetylcholinesterase (AChE) is responsible for the hydrolysis of the neurotransmitter, acetylcholine, in the nervous system. The functional localization and oligomerization of AChE T variant are depending primarily on the association of their anchoring partners, either collagen tail (ColQ) or proline-rich membrane anchor (PRiMA). Complexes with ColQ represent the asymmetric forms (A<sub>12</sub>) in muscle, while complexes with PRiMA represent tetrameric globular forms (G<sub>4</sub>) mainly found in brain and muscle. Apart from these traditional molecular forms, a ColQ-linked asymmetric form and a PRiMA-linked globular form of hybrid cholinesterases (ChEs), having both AChE and BChE catalytic subunits, were revealed in chicken brain and muscle. The similarity of various molecular forms of AChE and BChE raises interesting question regarding to their possible relationship in enzyme assembly and localization. The focus of this review is to provide current findings about the biosynthesis of different forms of ChEs together with their anchoring proteins.</p>