Differential mRNA expression and protein localization of the SAP90/PSD-95-associated proteins (SAPAPs) in the nervous system of the mouse - PubMed (original) (raw)

Comparative Study

. 2004 Apr 19;472(1):24-39.

doi: 10.1002/cne.20060.

Affiliations

• PMID: 15024750
• DOI: 10.1002/cne.20060

Comparative Study

Differential mRNA expression and protein localization of the SAP90/PSD-95-associated proteins (SAPAPs) in the nervous system of the mouse

Jeffrey M Welch et al. J Comp Neurol. 2004.

Abstract

The supramolecular anchoring/signaling complex at the postsynaptic density of glutamatergic synapses has been proposed to play a key role in regulating synaptic function and plasticity. One class of proteins present in the complex is the SAP90/PSD-95-associated protein family (SAPAPs). The SAPAPs, identified by their direct interaction with PSD-95 family proteins, were initially proposed to function in the anchoring/signaling complex as linker proteins between glutamate receptor binding proteins and the cytoskeleton. However, recent studies have indicated that the SAPAPs also bind to signaling molecules and may thus have multiple roles at synapses. Four homologous genes encoding SAPAP proteins have been previously identified. As a first step toward understanding the physiological function of the SAPAPs, we have investigated in detail, at both the mRNA and protein levels, the localization of the individual SAPAP genes in the adult murine nervous system. We find that the SAPAP mRNAs are highly, yet differentially, expressed in many regions of the brain, including the hippocampus and cerebellum. Furthermore, SAPAP3 mRNA is targeted to dendrites, whereas SAPAP1, -2, and -4 mRNAs are detected mainly in cell bodies. The SAPAP proteins are localized at synapses in a manner consistent with mRNA expression. Surprisingly, in addition to glutamatergic synapse localization, antibody staining also reveals that the SAPAP proteins are localized at cholinergic synapses, including neuronal cholinergic synapses and the neuromuscular junction. Together, these results indicate that the SAPAPs are general components of excitatory synapses and that each of these proteins may perform a distinct function.

Copyright 2004 Wiley-Liss, Inc.

PubMed Disclaimer

Similar articles

• Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family.
  Boeckers TM, Winter C, Smalla KH, Kreutz MR, Bockmann J, Seidenbecher C, Garner CC, Gundelfinger ED. Boeckers TM, et al. Biochem Biophys Res Commun. 1999 Oct 14;264(1):247-52. doi: 10.1006/bbrc.1999.1489. Biochem Biophys Res Commun. 1999. PMID: 10527873
• Characterization of mRNA species that are associated with postsynaptic density fraction by gene chip microarray analysis.
  Suzuki T, Tian QB, Kuromitsu J, Kawai T, Endo S. Suzuki T, et al. Neurosci Res. 2007 Jan;57(1):61-85. doi: 10.1016/j.neures.2006.09.009. Epub 2006 Oct 17. Neurosci Res. 2007. PMID: 17049655
• SAPAP Scaffold Proteins: From Synaptic Function to Neuropsychiatric Disorders.
  Bai Y, Wang H, Li C. Bai Y, et al. Cells. 2022 Nov 28;11(23):3815. doi: 10.3390/cells11233815. Cells. 2022. PMID: 36497075 Free PMC article. Review.
• Postsynaptic density-membrane associated guanylate kinase proteins (PSD-MAGUKs) and their role in CNS disorders.
  Gardoni F, Marcello E, Di Luca M. Gardoni F, et al. Neuroscience. 2009 Jan 12;158(1):324-33. doi: 10.1016/j.neuroscience.2008.07.068. Epub 2008 Aug 13. Neuroscience. 2009. PMID: 18773944 Review.

Cited by

• Cortico-striatal synaptic defects and OCD-like behaviours in Sapap3-mutant mice.
  Welch JM, Lu J, Rodriguiz RM, Trotta NC, Peca J, Ding JD, Feliciano C, Chen M, Adams JP, Luo J, Dudek SM, Weinberg RJ, Calakos N, Wetsel WC, Feng G. Welch JM, et al. Nature. 2007 Aug 23;448(7156):894-900. doi: 10.1038/nature06104. Nature. 2007. PMID: 17713528 Free PMC article.
• Quantitative DNA Methylation Analysis of DLGAP2 Gene using Pyrosequencing in Schizophrenia with Tardive Dyskinesia: A Linear Mixed Model Approach.
  Li Y, Wang K, Zhang P, Huang J, An H, Wang N, De Yang F, Wang Z, Tan S, Chen S, Tan Y. Li Y, et al. Sci Rep. 2018 Nov 30;8(1):17466. doi: 10.1038/s41598-018-35718-4. Sci Rep. 2018. PMID: 30504779 Free PMC article.
• Dlgap1 knockout mice exhibit alterations of the postsynaptic density and selective reductions in sociability.
  Coba MP, Ramaker MJ, Ho EV, Thompson SL, Komiyama NH, Grant SGN, Knowles JA, Dulawa SC. Coba MP, et al. Sci Rep. 2018 Feb 2;8(1):2281. doi: 10.1038/s41598-018-20610-y. Sci Rep. 2018. PMID: 29396406 Free PMC article.
• Astrocyte-neuron subproteomes and obsessive-compulsive disorder mechanisms.
  Soto JS, Jami-Alahmadi Y, Chacon J, Moye SL, Diaz-Castro B, Wohlschlegel JA, Khakh BS. Soto JS, et al. Nature. 2023 Apr;616(7958):764-773. doi: 10.1038/s41586-023-05927-7. Epub 2023 Apr 12. Nature. 2023. PMID: 37046092 Free PMC article.
• The DLGAP family: neuronal expression, function and role in brain disorders.
  Rasmussen AH, Rasmussen HB, Silahtaroglu A. Rasmussen AH, et al. Mol Brain. 2017 Sep 4;10(1):43. doi: 10.1186/s13041-017-0324-9. Mol Brain. 2017. PMID: 28870203 Free PMC article. Review.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Wiley

• Molecular Biology Databases

  • BioCyc
  • Gene Ontology
  • GlyGen glycoinformatics resource
  • Mouse Genome Informatics (MGI)

• Research Materials

  • NCI CPTC Antibody Characterization Program