Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family.
We have recently isolated a novel proline-rich synapse-associated protein-1 (ProSAP1) that is highly enriched in postsynaptic density (PSD). A closely related multidomain protein, ProSAP2, shares a highly conserved PDZ (PSD-95/discs-large/ZO-1) domain (80% identity), a ppI domain that mediates the interaction with cortactin, and a C-terminal SAM (sterile alpha-motif) domain. In ... addition, ProSAP2 codes for five ankyrin repeats and a SH3 (Src homology 3) domain. Transcripts for both proteins are coexpressed in many regions of rat brain, but show a distinct expression pattern in the cerebellum. Using the PDZ domains of ProSAP1 and 2 as bait in the yeast two-hybrid system, we isolated several clones of the SAPAP/GKAP (SAP90/PSD-95-associated protein/guanylate kinase-associated protein) family. The association of the proteins was verified by coimmunoprecipitation and cotransfection in HEK cells. Therefore, proteins of the ProSAP family represent a novel link between SAP90/PSD-95 bound membrane receptors and the cytoskeleton at glutamatergic synapses of the central nervous system.
Mesh Terms:
Amino Acid Sequence, Animals, Brain, Carrier Proteins, Cytoskeleton, Molecular Sequence Data, Nerve Tissue Proteins, Rats, Sequence Homology, Amino Acid, Synaptic Membranes
Amino Acid Sequence, Animals, Brain, Carrier Proteins, Cytoskeleton, Molecular Sequence Data, Nerve Tissue Proteins, Rats, Sequence Homology, Amino Acid, Synaptic Membranes
Biochem. Biophys. Res. Commun.
Date: Oct. 14, 1999
PubMed ID: 10527873
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