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PMID:16522626

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Citation

Wendholt, D, Spilker, C, Schmitt, A, Dolnik, A, Smalla, KH, Proepper, C, Bockmann, J, Sobue, K, Gundelfinger, ED, Kreutz, MR and Boeckers, TM (2006) ProSAP-interacting protein 1 (ProSAPiP1), a novel protein of the postsynaptic density that links the spine-associated Rap-Gap (SPAR) to the scaffolding protein ProSAP2/Shank3. J. Biol. Chem. 281:13805-16

Abstract

ProSAPs/Shanks are a family of proteins that have a major scaffolding function for components of the postsynaptic density (PSD) of excitatory brain synapses. Members of the family harbor a variety of domains for protein-protein interactions, one of which is a unique PDZ domain that differs significantly from those of other proteins. We have identified a novel binding partner for this PDZ domain, termed ProSAPiP1, that is highly enriched in the PSD and shares significant sequence homology with the PSD protein PSD-Zip70. Both molecules code for a Fez1 domain that can be found in a total of four related proteins. ProSAPiP1 is widely expressed in rat brain and co-localizes with ProSAP2/Shank3 in excitatory spines and synapses. ProSAP2/Shank3 co-immunoprecipitates with ProSAPiP1 but not with PSD-Zip70. Both proteins, however, bind and recruit SPAR to synapses with a central coiled-coil region that harbors a leucine zipper motif. This region is also responsible for homo- and heteromultimerization of ProSAPiP1 and PSD-Zip70. Thus, ProSAPiP1 and PSD-Zip70 are founders of a novel family of scaffolding proteins, the "Fezzins," which adds further complexity to the organization of the PSD protein network.

Links

PubMed Online version:10.1074/jbc.M601101200

Keywords

Adaptor Proteins, Signal Transducing/metabolism; Animals; Binding Sites; Brain/cytology; Brain/metabolism; COS Cells; Cells, Cultured; Cercopithecus aethiops; GTPase-Activating Proteins/metabolism; Molecular Sequence Data; Nerve Tissue Proteins/metabolism; Neurons/cytology; Neurons/metabolism; Protein Binding; Protein Structure, Tertiary; Protein Transport; Rats

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

RAT:SI1L1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8K1Q4

F

Seeded From UniProt

complete

RAT:SI1L1

located_in

GO:0014069: postsynaptic density

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

RAT:LZTS3

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:O35412

F

Seeded From UniProt

complete

RAT:LZTS3

enables

GO:0030165: PDZ domain binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9JLU4

F

Seeded From UniProt

complete

RAT:LZTS3

located_in

GO:0014069: postsynaptic density

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

RAT:LZTS3

located_in

GO:0043197: dendritic spine

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

RAT:LZTS3

involved_in

GO:0051260: protein homooligomerization

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8K1Q4

P

Seeded From UniProt

complete

RAT:LZTS3

enables

GO:0043621: protein self-association

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8K1Q4

F

Seeded From UniProt

complete

RAT:SHAN3

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8K1Q4

F

Seeded From UniProt

complete

RAT:SHAN3

located_in

GO:0014069: postsynaptic density

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

RAT:SHAN3

part_of

GO:0014069: postsynaptic density

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete


See also

References

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