Acetylcholinesterase collagenic tail peptide (ColQ) (COLQ)

Acetylcholinesterase collagenic tail peptide (ColQ) is a structural protein essential for the organization of the neuromuscular junction (NMJ) (UniProt: P19405). It functions by anchoring the asymmetric form of acetylcholinesterase (AChE) to the synaptic basal lamina, ensuring that the enzyme is correctly positioned to terminate neurotransmission by hydrolyzing acetylcholine (PubMed: 10446163). Mutations in the COLQ gene lead to endplate acetylcholinesterase deficiency, a subtype of congenital myasthenic syndrome (CMS) characterized by muscle weakness and fatigability (OMIM: 603033). Without functional ColQ, AChE is absent from the synaptic cleft, resulting in prolonged acetylcholine residence and potential excitotoxic damage to the postsynaptic membrane (StatPearls: Congenital Myasthenic Syndrome). Therapeutic approaches currently focus on symptomatic management using beta-2 adrenergic agonists like salbutamol or ephedrine, which improve NMJ stability (PubMed: 25103055). Emerging treatments include gene therapy aimed at delivering a functional COLQ gene to restore enzyme anchoring and normal synaptic function (PubMed: 22962327).

Other names

Collagen-like tail subunit of asymmetric acetylcholinesteraseAcetylcholinesterase-associated collagenCOLQAChE Q subunit

Therapeutic strategies involve the restoration of acetylcholinesterase anchoring at the motor endplate through gene replacement or the use of beta-2 adrenergic agonists to stabilize the neuromuscular junction and improve synaptic transmission (PubMed: 25103055, 22962327).