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Article

Dok-7 regulates neuromuscular synapse formation by recruiting Crk and Crk-L.

Genes & development - 1 Nov 2010

Hallock Peter T, Xu Chong-Feng, Park Tae-Ju, Neubert Thomas A, Curran Tom, Burden Steven J

Abstract excerpt

Agrin, released by motor neurons, promotes neuromuscular synapse formation by stimulating MuSK, a receptor tyrosine kinase expressed in skeletal muscle. Phosphorylated MuSK recruits docking protein-7 (Dok-7), an adaptor protein that is expressed selectively in muscle. In the absence of Dok-7, neuromuscular synapses fail to form, and mutations that impair Dok-7 are a major cause of congenital myasthenia in humans....

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Share to Muscle Fibers, Skeletal
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muscle Proteins

Share to Neuromuscular Junction

Share to Receptor Protein-Tyrosine Kinases

Share to Receptors, Cholinergic

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Source

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Identifiers

PMID: 21041412
DOI: 10.1101/gad.1977710
PMCID: PMC2964755

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Dok-7 regulates neuromuscular synapse formation by recruiting Crk and Crk-L.PMID 21041412Read ↗

The muscle protein Dok-7 is essential for neuromuscular synaptogenesis.Semantic proximity Read ↗

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Mechanism of disease and therapeutic rescue of Dok7 congenital myasthenia.Semantic proximity Read ↗

Dok-7/MuSK signaling and a congenital myasthenic syndrome.Semantic proximity Read ↗

The cytoplasmic adaptor protein Dok7 activates the receptor tyrosine kinase MuSK via dimerization.Semantic proximity Read ↗

The synaptic muscle‐specific kinase (MuSK) complex: New partners, new functionsSemantic proximity Read ↗

Sorbs1 and -2 Interact with CrkL and Are Required for Acetylcholine Receptor Cluster Formation.Semantic proximity Read ↗

Dok-7 promotes slow muscle integrity as well as neuromuscular junction formation in a zebrafish model of congenital myasthenic syndromesSemantic proximity Read ↗

Distinct domains of MuSK mediate its abilities to induce and to associate with postsynaptic specializations.Semantic proximity Read ↗

Congenital myasthenic syndrome due to mutations in MUSK suggests that the level of MuSK phosphorylation is crucial for governing synaptic structure.Semantic proximity Read ↗

Mutations in MUSK causing congenital myasthenic syndrome impair MuSK–Dok-7 interactionSemantic proximity Read ↗

A mechanism in agrin signaling revealed by a prevalent Rapsyn mutation in congenital myasthenic syndromeSemantic proximity Read ↗

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