Collagen-like tail subunit of asymmetric acetylcholinesterase (COLQ) (COLQ)

Collagen Q (COLQ) is a specialized structural protein that plays a critical role in the organization and functionality of the neuromuscular junction (NMJ). Its primary biological role is to anchor the catalytic subunits of acetylcholinesterase (AChE) to the synaptic basal lamina, ensuring that the enzyme is correctly positioned to terminate nerve impulse transmission by rapidly hydrolyzing acetylcholine (UniProt: P54803). This anchoring is achieved through the interaction of the COLQ C-terminal domain with the MuSK-LRP4 receptor complex and the N-terminal proline-rich attachment domain (PRAD) with AChE tetramers (PubMed: 11514519). Mutations in the COLQ gene lead to a specific form of congenital myasthenic syndrome (CMS) characterized by endplate acetylcholinesterase deficiency, which results in prolonged synaptic currents, endplate myopathy, and severe muscle weakness (PubMed: 9662394). Because COLQ is essential for the functional localization of AChE, it is a primary target for genetic therapies, such as AAV-mediated gene delivery, aimed at restoring NMJ function (PubMed: 28810573). While traditional pharmacological treatments like salbutamol and ephedrine are used to manage symptoms by stabilizing the NMJ, they do not directly replace the missing COLQ protein.

Other names

Acetylcholinesterase collagenic tail peptideCollagen QCMS5EADSingle strand of asymmetric acetylcholinesterase

Anchoring of acetylcholinesterase (AChE) to the synaptic basal lamina at the neuromuscular junction via binding to the MuSK-LRP4 complex (PubMed: 11514519).