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

NMDA receptors are linked to intracellular cytoskeletal and signaling molecules via the PSD-95 protein complex. We report a novel family of postsynaptic density (PSD) proteins, termed Shank, that binds via its PDZ domain to the C terminus of PSD-95-associated protein GKAP. A ternary complex of Shank/GKAP/PSD-95 assembles in heterologous cells and can be coimmunoprecipitated from rat brain. Synaptic localization of Shank in neurons is inhibited by a GKAP splice variant that lacks the Shank-binding C terminus. In addition to its PDZ domain, Shank contains a proline-rich region that binds to cortactin and a SAM domain that mediates multimerization. Shank may function as a scaffold protein in the PSD, potentially cross-linking NMDA receptor/PSD-95 complexes and coupling them to regulators of the actin cytoskeleton.

Pubmed ID: 10433268


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



Publication Data

July 13, 1999

Associated Grants

  • Agency: NIDA NIH HHS, Id: DA103009
  • Agency: NINDS NIH HHS, Id: NS29879
  • Agency: NINDS NIH HHS, Id: NS35050

Mesh Terms

  • Actins
  • Adaptor Proteins, Signal Transducing
  • Animals
  • COS Cells
  • Carrier Proteins
  • Cortactin
  • Cytoskeleton
  • Hippocampus
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • Microscopy, Immunoelectron
  • Molecular Sequence Data
  • Multigene Family
  • Nerve Tissue Proteins
  • Neurons
  • Protein Structure, Tertiary
  • Rabbits
  • Rats
  • Receptors, N-Methyl-D-Aspartate
  • Sequence Homology, Amino Acid
  • Synapses