From Protein to Peptides: a Spectrum of Non-Hydrolytic Functions of Acetylcholinesterase

Amy      C. Halliday; Susan      A. Greenfield

doi:10.2174/092986612799080149

Abstract

Acetylcholinesterase (AChE), a member of the α/β-hydrolase fold superfamily of proteins, is a serine hydrolase responsible for the hydrolysis of the well studied neurotransmitter acetylcholine (ACh). However, it is becoming clear that AChE has a range of actions other than this ‘classical’ role. Non-classical AChE functions have been identified in apoptosis, stress-responses, neuritogenesis, and neurodegeneration. Furthermore, these non-classical roles are attributable not only to the native protein, which appears to act as a mediary binding protein under a number of circumstances, but also to peptides cleaved from the parent protein. Peptides cleaved from AChE can act as independent signalling molecules. Here we discuss the implications of non-hydrolytic functions of this multi-tasking protein.

Keywords: Acetylcholinesterase, adhesion, apoptosis, neurogenesis, non-hydrolytic function, signalling peptide, synaptic, exons, Tetramers, 3D X-ray structure, glycophosphatidylinositol (GPI)