Acetylcholinesterase: C-terminal domains,molecular forms and functional localization |
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| Institution: | 1. Department of Toxicology and Military Pharmacy, Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic;2. Biomedical Research Centre, University Hospital, Hradec Kralove, Czech Republic;3. Department of Clinical Biochemistry, University Hospital, Hradec Kralove, Czech Republic;4. Department of Chemistry, Faculty of Science, University of Hradec Kralove, Hradec Kralove, Czech Republic;5. Department of Cellular Biology and Pharmacology, Florida International University, Miami, FL, USA;1. Department of Pharmacy, Gansu Provincial Hospital, Lanzhou 730000, Gansu, China;2. Division of Oncology, Gansu Provincial Hospital, Lanzhou 730000, Gansu, China;1. Division of Crop Protection, National Academy of Agricultural Science, Rural Development Administration, Jeollabuk-do 55365, Republic of Korea;2. Department of Agricultural Biotechnology, Seoul National University, Seoul 151-742, Republic of Korea;3. Research Institute of Agriculture and Life Science, Seoul National University, Seoul 151-742, Republic of Korea |
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| Abstract: | Acetylcholinesterase (AChE) possesses short C-terminal peptides that are not necessary for catalytic activity. These peptides belong to different classes (R, H, T, S) and define the post-translational processing and targeting of the enzyme. In vertebrates, subunits of type H (AChEH) and of type T (AChET) are the most important: AChEH subunits produced glycolipid (GPI)-anchored dimers and AChET subunits produce hetero-oligometric forms such as membrane-bound tetramer in the mammalian brain (containing a 20 kDa hydrophobic protein) and asymmetric collagen-tailed forms in neuromuscular junctions (containing a specific collagen, ColQ). The T peptide allows the formation of tetrameric assemblies with a proline-rich attachment domain (PRAD) of collagen ColQ. These complex molecular structures condition the functional localization of the enzyme in the supramolecular architecture of cholinegic synapses. |
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