GoPubMed Proteins lists recent and important papers and reviews for
proteins. Page last changed on 14 Mar 2013.
Collagen-like tail subunit
ColQ
This gene encodes the subunit of a collagen-like molecule associated with acetylcholinesterase in skeletal muscle. Each molecule is composed of three identical subunits. Each subunit contains a proline-rich attachment domain (PRAD) that binds an acetylcholinesterase tetramer to anchor the catalytic subunit of the enzyme to the basal lamina. Mutations in this gene are associated with endplate acetylcholinesterase deficiency. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from
NCBI)
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Papers on
ColQ
Polyproline tetramer organizing peptides in fetal bovine serum acetylcholinesterase.
New
Ankara, Turkey. In Biochim Biophys Acta, 30 Apr 2013
A search of the mammalian proteome database suggested that this assortment of polyproline peptides originated from at least 5 different precursor proteins, none of which were the ColQ or PRiMA of membrane-anchored AChE.
Synaptic basal lamina-associated congenital myasthenic syndromes.
Review
New
Davis, United States. In Ann N Y Acad Sci, Dec 2012
Most important junctional BL proteins are collagens, such as collagen IV (α3-6), collagen XIII, and ColQ; laminins; nidogens; and heparan sulfate proteoglycans, such as perlecan and agrin.
Expression of cAMP-responsive element binding proteins (CREBs) in fast- and slow-twitch muscles: A signaling pathway to account for the synaptic expression of collagen-tailed subunit (ColQ) of acetylcholinesterase at the rat neuromuscular junction.
New
Hong Kong, Hong Kong. In Chem Biol Interact, Dec 2012
The gene encoding the collagen-tailed subunit (ColQ) of acetylcholinesterase (AChE) contains two distinct promoters that drive the production of two ColQ mRNAs, ColQ-1 and ColQ-1a, in slow- and fast-twitch muscles, respectively.
Acetylcholinesterase and Agrin: Different Functions, Similar Expression Patterns, Multiple Roles.
New
Ljubljana, Slovenia. In Chem Biol Interact, Nov 2012
However, while the origin of basal lamina bound agrin is undoubtedly neural, the neural origin of AChE, which is anchored to the basal lamina with collagenic tail ColQ, is elusive.
Developmental consequences of the ColQ/MuSK interactions.
New
Paris, France. In Chem Biol Interact, Nov 2012
CollagenQ (ColQ) is a specific collagen that anchors acetylcholinesterase (AChE) in the synaptic basal lamina of the neuromuscular junction (NMJ).
Specific binding of collagen Q to the neuromuscular junction is exploited to cure congenital myasthenia and to explore bases of myasthenia gravis.
New
Nagoya, Japan. In Chem Biol Interact, Oct 2012
Acetylcholinesterase (AChE) at the neuromuscular junction (NMJ) is anchored to the synaptic basal lamina via a triple helical collagen Q (ColQ) in the form of asymmetric AChE (AChE/ColQ).
Near-complete adaptation of the PRiMA knockout to the lack of central acetylcholinesterase.
New
Paris, France. In J Neurochem, Sep 2012
Since PRiMA-KO mice and AChE-deficient mice have similar low AChE concentrations in the brain but differ in the AChE content of the peripheral nervous system, these results suggest that peripheral nervous system AChE is a major target of AChE inhibitors, and that its absence in AChE- deficient mice is the main cause of the slow development and vulnerability of these mice.
Suppression of collagen Q expression in the extrajunctional regions of rat fast muscles is encoded in their stem cells (satellite cells).
New
Ljubljana, Slovenia. In Chem Biol Interact, Sep 2012
In rat fast muscles, collagen Q (ColQ) expression is restricted to the neuromuscular junctions.
Recurrent COLQ mutation in congenital myasthenic syndrome.
New
Ankara, Turkey. In Pediatr Neurol, Apr 2012
Mutations in the COLQ gene result in acetylcholinesterase deficiency and cause a rare, autosomal recessive synaptic form of congenital myasthenic syndrome, with variable age of onset and clinical severity.
Congenital myasthenic syndrome: a brief review.
Review
New
Curitiba, Brazil. In Pediatr Neurol, Mar 2012
Therefore, genetic testing may be necessary to identify specific mutations in CHAT, COLQ, LAMB2, CHRNA, CHRNB, CHRND, CHRNE, CHRNG, RAPSN, DOK7, MUSK, AGRN, SCN4A, GFPT1, or PLEC1 genes.
[Congenital myasthenic syndromes].
Nagoya, Japan. In Rinsho Shinkeigaku, 2011
Third, collagen Q (ColQ) anchors acetylcholinesterase (AChE) to the synaptic basal lamina and mutations in COLQ lead to endplate AChE deficiency.
[Anti-MuSK antibodies in myasthenia gravis block binding of collagen Q to MuSK].
Nagoya, Japan. In Rinsho Shinkeigaku, 2011
MuSK also anchors the collagenic tail subunit (ColQ) of acetylcholinesterase (AChE).
Role of extracellular matrix proteins and their receptors in the development of the vertebrate neuromuscular junction.
Review
Columbus, United States. In Dev Neurobiol, 2011
Biochemical, genetic, and microscopy studies have confirmed that agrin, laminin (221, 421, and 521), collagen IV (α3-α6), collagen XIII, perlecan, and the ColQ-bound form of acetylcholinesterase are all synaptic ECM proteins with important roles in neuromuscular development.
Distinct localization of collagen Q and PRiMA forms of acetylcholinesterase at the neuromuscular junction.
GeneRIF
Paris, France. In Mol Cell Neurosci, 2011
Data show that along the nerve terminus the vast majority of acetylcholinesterase is anchored by collagen Q that is only produced by the muscle, whereas very minor amounts of AChE are anchored by PRiMA that is produced by motoneurons.
Intra-familial variation in clinical manifestations and response to ephedrine in siblings with congenital myasthenic syndrome caused by novel COLQ mutations.
GeneRIF
In Dev Med Child Neurol, 2010
two siblings have identical novel heterozygous mutations but different phenotypic expressions.
Cholinesterases regulation in the absence of ColQ.
GeneRIF
Paris, France. In Chem Biol Interact, 2010
AChE, BChE and PRiMA mRNA level modifications found in the absence of ColQ cannot compensate for the physiological defects observed at the ColQ-deficient neuromuscular junction.
The asymmetric molecular forms of AChE and the expression of collagen Q in mature and immature fast and slow rat muscles.
GeneRIF
Ljubljana, Slovenia. In Chem Biol Interact, 2010
extrajunctional levels of ColQ mRNA in non-innervated regenerating fast and slow muscles
ColQ controls postsynaptic differentiation at the neuromuscular junction.
GeneRIF
Paris, France. In J Neurosci, 2010
In addition to its structural role, ColQ has important regulatory functions at the synapse by controlling acetylcholine receptor clustering through its interaction with MuSK.
What have we learned from the congenital myasthenic syndromes.
Review
Rochester, United States. In J Mol Neurosci, 2010
For example, electrophysiologic studies in patients suffering from sudden episodes of apnea pointed to a defect in acetylcholine resynthesis and CHAT as the candidate gene (Ohno et al., Proc Natl Acad Sci USA 98:2017-2022, 2001); refractoriness to anticholinesterase medications and partial or complete absence of acetylcholinesterase (AChE) from the endplates (EPs) has pointed to one of the two genes (COLQ and ACHE ( T )) encoding AChE, though mutations were observed only in COLQ.
[Molecular bases and therapeutic strategies in defective neuromuscular transmissions: lessons learned from a prototypical synapse].
Review
Nagoya, Japan. In Nihon Shinkei Seishin Yakurigaku Zasshi, 2009
(2) Collagen Q (ColQ) anchors acetylcholinesterase at the synaptic basal lamina, and its defects cause endplate acetylcholinesterase deficiency.
