Shank binds Gkap1

Stable Identifier
Reaction [binding]
Rattus norvegicus
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
10806096 The Shank family of scaffold proteins

Sheng, M, Kim, E

J. Cell. Sci. 2000
10433268 Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin

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

Neuron 1999
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

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

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

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

J. Cell Biol. 1997
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