Collagen Q (ColQ)

Collagen Q (ColQ) is a specialized, nonfibrillar collagen found at the vertebrate neuromuscular junction (NMJ). Its primary function is to anchor acetylcholinesterase (AChE) in the synaptic basal lamina, enabling efficient breakdown of synaptic acetylcholine and termination of neurotransmission[1][6]. ColQ forms part of the asymmetric (collagen-tailed) forms of AChE, essential for normal neuromuscular signaling. It also interacts with low-density lipoprotein receptor–related protein 4 (LRP4), indirectly influencing the muscle-specific kinase (MuSK)–LRP4 receptor complex, which is vital for acetylcholine receptor clustering and synaptic gene expression regulation at the NMJ[1]. Genetic disruption of ColQ results in the absence of AChE at NMJs, causing severe impairment in synaptic function and leading to neuromuscular diseases such as congenital myasthenic syndromes[6]. ColQ is not a classic therapeutic receptor or enzyme, but is essential for synaptic integrity and is indirectly a therapeutic target in neuromuscular junction disorders[1][6].

Other names

Collagen-like tail subunit of acetylcholinesteraseColQAChE collagen subunit

Anchors acetylcholinesterase to the synaptic basal lamina; influences synaptic AChE localization and stability; modulates acetylcholine receptor clustering via interaction with LRP4 and downstream signaling