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Shank2  -  SH3 and multiple ankyrin repeat domains 2

Rattus norvegicus

Synonyms: CortBP1, Cortactin-binding protein 1, Cortbp1, GKAP/SAPAP-interacting protein, ProSAP1, ...
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High impact information on Shank2


Biological context of Shank2

  • The present study utilized bioinformatics to demonstrate the presence of exons encoding ankyrin repeats in the region preceding the previously described Shank2 gene. cDNA sequencing of mRNA from epithelial cells revealed a novel spliceoform of Shank2, termed Shank2E, that encodes a predicted 200 kDa protein with six N-terminal ankyrin repeats [4].
  • The association between SSTR2 and the PDZ-domain of CortBP1 was verified by overlay assays and by coprecipitation after transfection in human embryonic kidney (HEK) cells [5].
  • CBP90 was purified from rat brain and its cDNA was cloned from a rat brain cDNA library [6].
  • The deduced amino acid sequence of CBP90 had no significant similarity to any other protein, but it had a proline-rich domain at the C-terminal region [6].
  • As a result of our ongoing studies on the distribution and function of this novel PDZ domain protein, we now report that the expression of ProSAP1 is restricted neither to neurons and interneuronal junctions nor to the nervous system [7].

Anatomical context of Shank2


Other interactions of Shank2

  • We studied the synaptic targeting of multi-domain proteins of the ProSAP/Shank family thought to serve as master scaffolding molecules of the postsynaptic density [12].
  • The double-labeling experiments revealed a high rate of colocalization of ProSAP1/Shank2 with Homer1 and PSD-95, and little colocalization with GRIP [9].
  • Importantly, different paradigms of neuronal stimulation induce a redistribution of Abp1 to ProSAP-containing synapses [11].
  • Our data suggest that IRSp53 can be recruited to the PSD via its ProSAP/Shank interaction and may contribute to the morphological reorganization of spines and synapses after insulin receptor and/or Cdc42Hs activation [10].

Analytical, diagnostic and therapeutic context of Shank2


  1. Identification of a novel cortactin SH3 domain-binding protein and its localization to growth cones of cultured neurons. Du, Y., Weed, S.A., Xiong, W.C., Marshall, T.D., Parsons, J.T. Mol. Cell. Biol. (1998) [Pubmed]
  2. Proline-rich synapse-associated protein-1/cortactin binding protein 1 (ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the postsynaptic density. Boeckers, T.M., Kreutz, M.R., Winter, C., Zuschratter, W., Smalla, K.H., Sanmarti-Vila, L., Wex, H., Langnaese, K., Bockmann, J., Garner, C.C., Gundelfinger, E.D. J. Neurosci. (1999) [Pubmed]
  3. The interaction of phospholipase C-beta3 with Shank2 regulates mGluR-mediated calcium signal. Hwang, J.I., Kim, H.S., Lee, J.R., Kim, E., Ryu, S.H., Suh, P.G. J. Biol. Chem. (2005) [Pubmed]
  4. Characterization of an ankyrin repeat-containing Shank2 isoform (Shank2E) in liver epithelial cells. McWilliams, R.R., Gidey, E., Fouassier, L., Weed, S.A., Doctor, R.B. Biochem. J. (2004) [Pubmed]
  5. Agonist-dependent interaction of the rat somatostatin receptor subtype 2 with cortactin-binding protein 1. Zitzer, H., Richter, D., Kreienkamp, H.J. J. Biol. Chem. (1999) [Pubmed]
  6. Isolation and characterization of cortactin isoforms and a novel cortactin-binding protein, CBP90. Ohoka, Y., Takai, Y. Genes Cells (1998) [Pubmed]
  7. The cortactin-binding postsynaptic density protein proSAP1 in non-neuronal cells. Redecker, P., Gundelfinger, E.D., Boeckers, T.M. J. Histochem. Cytochem. (2001) [Pubmed]
  8. Differential expression and dendritic transcript localization of Shank family members: identification of a dendritic targeting element in the 3' untranslated region of Shank1 mRNA. Böckers, T.M., Segger-Junius, M., Iglauer, P., Bockmann, J., Gundelfinger, E.D., Kreutz, M.R., Richter, D., Kindler, S., Kreienkamp, H.J. Mol. Cell. Neurosci. (2004) [Pubmed]
  9. The postsynaptic scaffold proteins ProSAP1/Shank2 and Homer1 are associated with glutamate receptor complexes at rat retinal synapses. Brandstätter, J.H., Dick, O., Boeckers, T.M. J. Comp. Neurol. (2004) [Pubmed]
  10. ProSAP/Shank postsynaptic density proteins interact with insulin receptor tyrosine kinase substrate IRSp53. Bockmann, J., Kreutz, M.R., Gundelfinger, E.D., Böckers, T.M. J. Neurochem. (2002) [Pubmed]
  11. Linkage of the actin cytoskeleton to the postsynaptic density via direct interactions of Abp1 with the ProSAP/Shank family. Qualmann, B., Boeckers, T.M., Jeromin, M., Gundelfinger, E.D., Kessels, M.M. J. Neurosci. (2004) [Pubmed]
  12. C-terminal synaptic targeting elements for postsynaptic density proteins ProSAP1/Shank2 and ProSAP2/Shank3. Boeckers, T.M., Liedtke, T., Spilker, C., Dresbach, T., Bockmann, J., Kreutz, M.R., Gundelfinger, E.D. J. Neurochem. (2005) [Pubmed]
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