Receptor-Associated Protein of The Synapse Proteins (RAPSN)

Human Receptor-Associated Protein of The Synapse (RAPSN) interaction partners

1. Report attributes the RAPSN mutation c.484G > A, identified in a homozygous state, to causing fetal akinesia deformation sequence.

2. Mutations in RAPSN and COLQ are the most common causes of congenital myasthenic syndrome in Israel.

3. Hypomethylation of CpG sites in RPTOR (show RPTOR Proteins), MGRN1 (show MGRN1 Proteins) and RAPSN in blood is associated with breast cancer.

4. These findings uncover a new link between rapsyn, lysosome positioning, exocytosis and plasma membrane integrity.

5. a mutation of the RAPSN gene may have a role in development of congenital myasthenic syndrome after general anaesthesia [case report]

6. Investigation of mutations in RAPSN determines that patients with congenital myasthenic syndrome can be misdiagnosed with seronegative myasthenia gravis.

7. An allelic quantification on patient's DNA identified three novel multi-exon deletions of RAPSN.

8. nAChR (show CHRNA4 Proteins) mobility in plasma membranes of myoblast cells during their differentiation to myotubes in the presence and absence of rapsyn

9. Rapsyn mutations in humans cause endplate acetylcholine-receptor (show CHRNA1 Proteins) deficiency and myasthenic syndrome

10. E-box mutations in the RAPSN promoter region may have a role in congenital myasthenic syndrome

Mouse (Murine) Receptor-Associated Protein of The Synapse (RAPSN) interaction partners

1. The RING domain of rapsyn contains E3 ligase activity. Mutation of the RING domain that abolishes the enzyme activity inhibits rapsyn- as well as agrin (show AGRN Proteins)-induced AChR clustering in heterologous and muscle cells. Further biological and genetic studies support a working model where rapsyn, a classic scaffold protein (show HOMER1 Proteins), serves as an E3 ligase to induce AChR clustering and NMJ formation, possibly by regulation of AChR neddylation

2. Protein kinase CK2 (show CSNK2A1 Proteins) interacts at the neuromuscular synapse with Rapsyn, Rac1, 14-3-3gamma (show YWHAG Proteins), and Dok-7 (show DOK7 Proteins) proteins and phosphorylates the latter two.

3. Plectin bridges acetylcholine receptors and intermediate filaments via direct interaction with the AChR-scaffolding protein rapsyn in an isoform-specific manner.

4. Molecular modelling, immunoprecipitation and bimolecular fluorescence complementation approaches identify an alpha-helical stretch of rapsyn to be crucial for binding to the dimerisation and docking domain of PKA type I.

5. typical anchoring proteins of central excitatory synapses coimmunoprecipitate and colocalize with rapsyn

6. alpha-Actinin (show ACTN1 Proteins), rapsyn, and surface AChR form a ternary complex.

7. nAChR (show CHRNA4 Proteins) mobility in plasma membranes of myoblast cells during their differentiation to myotubes in the presence and absence of rapsyn

8. These results provide the first experimental evidence that rapsyn is a direct sequence-specific target of Kaiso (show ZBTB33 Proteins) and delta-catenin (show CTNND2 Proteins).

9. Thus, the metabolic half-life of receptors at the synapse may be modulated by local changes in the subsynaptic ratio of rapsyn to AChR.

10. Remarkable dynamism of rapsyn underlies stability and maintenance of the postsynaptic scaffold and suggests that the insertion of different postsynaptic proteins may be operating independently.

Zebrafish Receptor-Associated Protein of The Synapse (RAPSN) interaction partners

1. Our findings indicate that the reduced postsynaptic receptor density resulting from defective rapsyn contributes to weakness, but is not solely responsible for use-dependent fatigue