PMID- 23637281
OWN - NLM
STAT- MEDLINE
DCOM- 20131219
LR  - 20211021
IS  - 1943-0264 (Electronic)
IS  - 1943-0264 (Linking)
VI  - 5
IP  - 5
DP  - 2013 May 1
TI  - The role of MuSK in synapse formation and neuromuscular disease.
PG  - a009167
LID - 10.1101/cshperspect.a009167 [doi]
LID - a009167
AB  - Muscle-specific kinase (MuSK) is essential for each step in neuromuscular synapse 
      formation. Before innervation, MuSK initiates postsynaptic differentiation, 
      priming the muscle for synapse formation. Approaching motor axons recognize the 
      primed, or prepatterned, region of muscle, causing motor axons to stop growing 
      and differentiate into specialized nerve terminals. MuSK controls presynaptic 
      differentiation by causing the clustering of Lrp4, which functions as a direct 
      retrograde signal for presynaptic differentiation. Developing synapses are 
      stabilized by neuronal Agrin, which is released by motor nerve terminals and 
      binds to Lrp4, a member of the low-density lipoprotein receptor family, 
      stimulating further association between Lrp4 and MuSK and increasing MuSK kinase 
      activity. In addition, MuSK phosphorylation is stimulated by an inside-out 
      ligand, docking protein-7 (Dok-7), which is recruited to tyrosine-phosphorylated 
      MuSK and increases MuSK kinase activity. Mutations in MuSK and in genes that 
      function in the MuSK signaling pathway, including Dok-7, cause congenital 
      myasthenia, and autoantibodies to MuSK, Lrp4, and acetylcholine receptors are 
      responsible for myasthenia gravis.
FAU - Burden, Steven J
AU  - Burden SJ
AD  - Molecular Neurobiology Program, Helen L. and Martin S. Kimmel Center for Biology 
      and Medicine at the Skirball Institute of Biomolecular Medicine, NYU Medical 
      School, New York, NY 10016, USA.
FAU - Yumoto, Norihiro
AU  - Yumoto N
FAU - Zhang, Wei
AU  - Zhang W
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20130501
PL  - United States
TA  - Cold Spring Harb Perspect Biol
JT  - Cold Spring Harbor perspectives in biology
JID - 101513680
RN  - 0 (Agrin)
RN  - 0 (LDL-Receptor Related Proteins)
RN  - 0 (LRP4 protein, human)
RN  - 0 (Receptors, Cholinergic)
RN  - EC 2.7.10.1 (MUSK protein, human)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Agrin/metabolism/physiology
MH  - Cell Differentiation
MH  - Humans
MH  - LDL-Receptor Related Proteins/chemistry/immunology/physiology
MH  - Models, Biological
MH  - Muscles/cytology/innervation/pathology
MH  - Myasthenia Gravis/*genetics/pathology
MH  - Myasthenic Syndromes, Congenital/*genetics/pathology
MH  - Protein Structure, Tertiary
MH  - Receptor Protein-Tyrosine Kinases/chemistry/immunology/*physiology
MH  - Receptors, Cholinergic/chemistry/immunology/*physiology
MH  - Synapses/*metabolism
PMC - PMC3632064
EDAT- 2013/05/03 06:00
MHDA- 2013/12/20 06:00
PMCR- 2015/05/01
CRDT- 2013/05/03 06:00
PHST- 2013/05/03 06:00 [entrez]
PHST- 2013/05/03 06:00 [pubmed]
PHST- 2013/12/20 06:00 [medline]
PHST- 2015/05/01 00:00 [pmc-release]
AID - 5/5/a009167 [pii]
AID - a009167 [pii]
AID - 10.1101/cshperspect.a009167 [doi]
PST - epublish
SO  - Cold Spring Harb Perspect Biol. 2013 May 1;5(5):a009167. doi: 
      10.1101/cshperspect.a009167.