DLG2

DLG2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases DLG2, PPP1R58, PSD-93, PSD93, chapsyn-110, discs large homolog 2, discs large MAGUK scaffold protein 2
External IDs MGI: 1344351 HomoloGene: 1046 GeneCards: DLG2
Genetically Related Diseases
obesity, nephroblastoma, Parkinson's disease[1]
RNA expression pattern


More reference expression data
Orthologs
Species Human Mouse
Entrez

1740

23859

Ensembl

ENSG00000150672

ENSMUSG00000052572

UniProt

Q15700

Q91XM9

RefSeq (mRNA)

NM_001243046
NM_001243047
NM_011807

RefSeq (protein)

NP_001136171.1
NP_001136172.1
NP_001136174.1
NP_001193698.1
NP_001355.2

NP_001229976.1
NP_035937.2

Location (UCSC) Chr 11: 83.46 – 85.63 Mb Chr 7: 91.09 – 92.45 Mb
PubMed search [2] [3]
Wikidata
View/Edit HumanView/Edit Mouse

Disks large homolog 2 (DLG2) also known as channel-associated protein of synapse-110 (chapsyn-110) or postsynaptic density protein 93 (PSD-93) is a protein that in humans is encoded by the DLG2 gene.[4][5]

Function

Chapsyn-110/PSD-93 a member of the membrane-associated guanylate kinase (MAGUK) family. The protein forms a heterodimer with a related family member that may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins. Alternatively spliced transcript variants encoding distinct isoforms have been described but their full-length nature has yet to be completely determined.[6]

Model organisms

Model organisms have been used in the study of DLG2 function. A knockout mouse line, called Dlg2tm1Dsb was generated.[14][15] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[12][16] Twenty four tests were carried out on homozygous mutant mice and five significant abnormalities were observed.[12] Both sexes had atypical indirect calorimetry and DEXA parameters. Females also had decreased body weight, decreased circulating HDL cholesterol levels, and increased susceptibility to bacterial infection.[12]

Interactions

DLG2 has been shown to interact with GRIN2B,[17][18] KCNJ12.[19]

References

  1. ↑ "Diseases that are genetically associated with DLG2 view/edit references on wikidata".
  2. ↑ "Human PubMed Reference:".
  3. ↑ "Mouse PubMed Reference:".
  4. ↑ Kim E, Cho KO, Rothschild A, Sheng M (December 1996). "Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins". Neuron. 17 (1): 103–13. doi:10.1016/S0896-6273(00)80284-6. PMID 8755482.
  5. ↑ Stathakis DG, Lee D, Bryant PJ (January 1999). "Fine-scale physical map of the 11q21 region surrounding the human DLG2 locus, the gene encoding Chapsyn-110". Genomics. 54 (1): 186–8. doi:10.1006/geno.1998.5527. PMID 9806853.
  6. ↑ "Entrez Gene: DLG2 discs, large homolog 2, chapsyn-110 (Drosophila)".
  7. ↑ "Body weight data for Dlg2". Wellcome Trust Sanger Institute.
  8. ↑ "Indirect calorimetry data for Dlg2". Wellcome Trust Sanger Institute.
  9. ↑ "DEXA data for Dlg2". Wellcome Trust Sanger Institute.
  10. ↑ "Clinical chemistry data for Dlg2". Wellcome Trust Sanger Institute.
  11. ↑ "Citrobacter infection data for Dlg2". Wellcome Trust Sanger Institute.
  12. 1 2 3 4 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  13. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  14. ↑ McGee AW, Topinka JR, Hashimoto K, Petralia RS, Kakizawa S, Kauer FW, Aguilera-Moreno A, Wenthold RJ, Kano M, Bredt DS, Kauer F (2001). "PSD-93 knock-out mice reveal that neuronal MAGUKs are not required for development or function of parallel fiber synapses in cerebellum". J. Neurosci. 21 (9): 3085–91. PMID 11312293.
  15. ↑ "Mouse Genome Informatics".
  16. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837Freely accessible. PMID 21722353.
  17. ↑ Inanobe A, Fujita A, Ito M, Tomoike H, Inageda K, Kurachi Y (June 2002). "Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses". Am. J. Physiol., Cell Physiol. 282 (6): C1396–403. doi:10.1152/ajpcell.00615.2001. PMID 11997254.
  18. ↑ Irie M, Hata Y, Takeuchi M, Ichtchenko K, Toyoda A, Hirao K, Takai Y, Rosahl TW, Südhof TC (September 1997). "Binding of neuroligins to PSD-95". Science. 277 (5331): 1511–5. doi:10.1126/science.277.5331.1511. PMID 9278515.
  19. ↑ Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR, Vandenberg CA (May 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. doi:10.1074/jbc.M400285200. PMID 15024025.

Further reading

  • Kim E, Niethammer M, Rothschild A, Jan YN, Sheng M (1995). "Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases.". Nature. 378 (6552): 85–8. doi:10.1038/378085a0. PMID 7477295. 
  • Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, Santillano DR, Wu Z, Huang F, Xia H, Peters MF, Froehner SC, Bredt DS (1996). "Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains.". Cell. 84 (5): 757–67. doi:10.1016/S0092-8674(00)81053-3. PMID 8625413. 
  • Hsueh YP, Kim E, Sheng M (1997). "Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95.". Neuron. 18 (5): 803–14. doi:10.1016/S0896-6273(00)80319-0. PMID 9182804. 
  • Niethammer M, Valtschanoff JG, Kapoor TM, Allison DW, Weinberg RJ, Craig AM, Sheng M (1998). "CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90.". Neuron. 20 (4): 693–707. doi:10.1016/S0896-6273(00)81009-0. PMID 9581762. 
  • Leonard AS, Davare MA, Horne MC, Garner CC, Hell JW (1998). "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit.". J. Biol. Chem. 273 (31): 19518–24. doi:10.1074/jbc.273.31.19518. PMID 9677374. 
  • Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain.". Cell. 94 (6): 773–82. doi:10.1016/S0092-8674(00)81736-5. PMID 9753324. 
  • Brenman JE, Topinka JR, Cooper EC, McGee AW, Rosen J, Milroy T, Ralston HJ, Bredt DS (1998). "Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A.". J. Neurosci. 18 (21): 8805–13. PMID 9786987. 
  • Craven SE, El-Husseini AE, Bredt DS (1999). "Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs.". Neuron. 22 (3): 497–509. doi:10.1016/S0896-6273(00)80705-9. PMID 10197530. 
  • Sans N, Petralia RS, Wang YX, Blahos J, Hell JW, Wenthold RJ (2000). "A developmental change in NMDA receptor-associated proteins at hippocampal synapses.". J. Neurosci. 20 (3): 1260–71. PMID 10648730. 
  • Garcia RA, Vasudevan K, Buonanno A (2000). "The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3596–601. doi:10.1073/pnas.070042497. PMC 16285Freely accessible. PMID 10725395. 
  • Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG (2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes.". Nat. Neurosci. 3 (7): 661–9. doi:10.1038/76615. PMID 10862698. 
  • Firestein BL, Craven SE, Bredt DS (2001). "Postsynaptic targeting of MAGUKs mediated by distinct N-terminal domains.". NeuroReport. 11 (16): 3479–84. doi:10.1097/00001756-200011090-00016. PMID 11095503. 
  • Haraguchi K, Satoh K, Yanai H, Hamada F, Kawabuchi M, Akiyama T (2001). "The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase.". Genes Cells. 5 (11): 905–911. doi:10.1046/j.1365-2443.2000.00374.x. PMID 11122378. 
  • DeMarco SJ, Strehler EE (2001). "Plasma membrane Ca2+-atpase isoforms 2b and 4b interact promiscuously and selectively with members of the membrane-associated guanylate kinase family of PDZ (PSD95/Dlg/ZO-1) domain-containing proteins.". J. Biol. Chem. 276 (24): 21594–600. doi:10.1074/jbc.M101448200. PMID 11274188. 
  • Russwurm M, Wittau N, Koesling D (2002). "Guanylyl cyclase/PSD-95 interaction: targeting of the nitric oxide-sensitive alpha2beta1 guanylyl cyclase to synaptic membranes.". J. Biol. Chem. 276 (48): 44647–52. doi:10.1074/jbc.M105587200. PMID 11572861. 
  • Weitzdoerfer R, Dierssen M, Fountoulakis M, Lubec G (2002). "Fetal life in Down syndrome starts with normal neuronal density but impaired dendritic spines and synaptosomal structure.". J. Neural Transm. Suppl. (61): 59–70. doi:10.1007/978-3-7091-6262-0_5. PMID 11771761. 
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