Shank binds Gkap1

Stable Identifier
R-RNO-6794350
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Shank binds Gkap1
PSD-95 interacts with GKAP through its GK domain (Kim et al. 1997). In turn, the C-terminus of GKAP binds to the Shank family of PDZ-containing scaffold proteins. The Shank family of proteins is highly enriched in the postsynaptic density (PSD) of excitatory synapses in brain. There are three known SHANK proteins: SHANK1, SHANK2, and SHANK3. SHANK contains multiple domains for protein-protein interactions, including ankyrin repeats, SH3 domain, PDZ domain, SAM domain, and an extensive proline-rich region (Sheng & Kim 2000). Shank may function as a scaffold protein in the PSD, potentially cross-linking NMDA receptor or Neuroligin:PSD-95 complexes and coupling them to regulators of the actin cytoskeleton (Naisbitt et al.1999).
Literature References
PubMed ID Title Journal Year
10433268 Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin

Sheng, M, Kim, E, Valtschanoff, J, Tu, JC, Naisbitt, S, Xiao, B, Weinberg, RJ, Sala, C, Worley, PF

Neuron 1999
10806096 The Shank family of scaffold proteins

Sheng, M, Kim, E

J. Cell. Sci. 2000
9221768 Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90

Sheng, M, Kim, E, Naisbitt, S, Yang, FC, Weinberg, RJ, Craig, AM, Rao, A

J. Neurosci. 1997
9024696 GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules

Sheng, M, Kim, E, Hsueh, YP, Rothschild, A, Naisbitt, S, Craig, AM, Rao, A

J. Cell Biol. 1997
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Orthologous Events
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