High impact information on Shank3

• Enhanced polyubiquitination of Shank3 and NMDA receptor in a mouse model of autism [1].
• Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins [2].
• Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin [3].
• The neuronal scaffold protein Shank3 mediates signaling and biological function of the receptor tyrosine kinase Ret in epithelial cells [4].
• Using the glutathione S-transferase pull-down assay and immunoprecipitation technique we demonstrated that the GluR1 subunit directly binds to the PDZ domain of Shank3 via its carboxyl terminal PDZ-binding motif [5].
• Mutation/deletion approaches indicate that these effects require interactions of Shank3 with the glutamate receptor complex [6].
• Here, we report that knock-down of Shank3/prolinerich synapse-associated protein-2 by RNA interference reduces spine density in hippocampal neurons [6].
• Moreover, transgene expression of Shank 3 is sufficient to induce functional dendritic spines in aspiny cerebellar neurons [6]

Mouse Models of Shank3

• Enhanced polyubiquitination of Shank3 and NMDA receptor in a mouse model of autism [1].

Associations of Shank3 with chemical compounds

• Direct interaction of post-synaptic density-95/Dlg/ZO-1 domain-containing synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor [5].

Regulatory relationships of Shank3

• Furthermore, we show that Ret9 but not Ret51 induces epithelial cells to form branched tubular structures in three-dimensional cultures in a Shank3-dependent manner [4].

References