Shank protein: Difference between revisions

[[Image:Shank Schematic.png|150px|left]]&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; [[Shank Family Proteins]] are scaffolding proteins found in the postsynaptic density (PSD) of excitatory synapses. The PSD, a structure within dendritic spines that is associated with the postsynaptic membrane, contains a complex assembly of proteins which organize neurotransmitter receptors, signaling pathways, and regulatory elements within a cytoskeletal matrix.<ref name="Park">PMID:12626503</ref> It aids the appropriate communication of incoming signals to cytoplasmic targets and contributes to neuronal plasticity by readily changing its composition and structure in response to neural activity.<ref name="Baron">PMID:16439662</ref> Shank proteins are believed to function as master organizer of the PSD owing to their ability to recruit and form multimeric complexes with postsynaptic receptors, signaling molecules and cytoskeletal proteins like AMPA, [[Neuroligin-Neurexin Interaction|Neuroligin]] and NMDA glutamate receptors.<ref name="Durand">PMID:17173049</ref>  Within the PSD, there are over 300 individual shank molecules in a single postsynaptic site, representing 5% of the total protein molecules and total protein mass of the PSD.<ref name="Bozdagi">PMID: 21167025</ref> Shanks contain five domains for protein-protein interactions, including an ankyrin repeat domain, used to bind acting regulating proteins, an Src homology 3 (Sh3) domain, used to bind AMPA receptors, a PDZ domain, used to bind G protein coupled receptors,  several proline-rich domains , and a C-terminal SAM domain, which is responsible for mediating Shank multimerization.<ref name="Park"/> Functionally, Shank is involved in the maturation and enlargement of dendritic spines and is able to induce spine formation in neurons.<ref name="Durand"/>