DLG2

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.[5][6]

DLG2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDLG2, PPP1R58, PSD-93, PSD93, chapsyn-110, discs large homolog 2, discs large MAGUK scaffold protein 2
External IDsOMIM: 603583 MGI: 1344351 HomoloGene: 1046 GeneCards: DLG2
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11q14.1Start83,455,012 bp[1]
End85,627,922 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

1740

23859

Ensembl

ENSG00000150672

ENSMUSG00000052572

UniProt

Q15700

Q91XM9

RefSeq (mRNA)

NM_001243046
NM_001243047
NM_011807

RefSeq (protein)

NP_001229975
NP_001229976
NP_035937

Location (UCSC)Chr 11: 83.46 – 85.63 MbChr 7: 90.48 – 92.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[7]

Model organisms

Model organisms have been used in the study of DLG2 function. A knockout mouse line, called Dlg2tm1Dsb was generated.[15][16] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][17] Twenty four tests were carried out on homozygous mutant mice and five significant abnormalities were observed.[13] 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.[13]

Interactions

DLG2 has been shown to interact with GRIN2B,[18][19] KCNJ12.[20]

References

  1. GRCh38: Ensembl release 89: ENSG00000150672 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000052572 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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. S2CID 14852857.
  6. 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.
  7. "Entrez Gene: DLG2 discs, large homolog 2, chapsyn-110 (Drosophila)".
  8. "Body weight data for Dlg2". Wellcome Trust Sanger Institute.
  9. "Indirect calorimetry data for Dlg2". Wellcome Trust Sanger Institute.
  10. "DEXA data for Dlg2". Wellcome Trust Sanger Institute.
  11. "Clinical chemistry data for Dlg2". Wellcome Trust Sanger Institute.
  12. "Citrobacter infection data for Dlg2". Wellcome Trust Sanger Institute.
  13. 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. S2CID 85911512.
  14. Mouse Resources Portal, Wellcome Trust Sanger Institute.
  15. 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. doi:10.1523/JNEUROSCI.21-09-03085.2001. PMC 6762564. PMID 11312293.
  16. "Mouse Genome Informatics".
  17. 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 3218837. PMID 21722353.
  18. 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.
  19. 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.
  20. 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

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.