DLG2

From Wikipedia, the free encyclopedia

Discs, large homolog 2, chapsyn-110 (Drosophila)

PDB rendering based on 1iu0.

Available structures: 1iu0, 1iu2, 2byg, 2he2

Identifiers

Symbol(s)

DLG2; DKFZp781D1854; DKFZp781E0954; FLJ37266; MGC131811; PSD-93

External IDs

OMIM: 603583 MGI: 1344351 HomoloGene: 1046

Gene ontology
Molecular Function:	• nucleic acid binding • guanylate kinase activity • pancreatic ribonuclease activity • protein binding
Cellular Component:	• plasma membrane • postsynaptic membrane
Biological Process:	• synaptic transmission • sensory perception of pain

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001364 (mRNA)
NP_001355 (protein)

NM_011807 (mRNA)
NP_035937 (protein)

Location

Chr 11: 82.85 - 84.67 Mb

Chr 7: 91.32 - 92.32 Mb

Pubmed search

[1]

[2]

Discs, large homolog 2, chapsyn-110 (Drosophila), also known as DLG2, is a human gene.

This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. The encoded 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.^[1]

[edit] References

^ Entrez Gene: DLG2 discs, large homolog 2, chapsyn-110 (Drosophila).

[edit] Further reading

Kim E, Niethammer M, Rothschild A, et al. (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, et al. (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. PMID 8625413.
Kim E, Cho KO, Rothschild A, Sheng M (1996). "Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins.". Neuron 17 (1): 103–13. PMID 8755482.
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. PMID 9182804.
Irie M, Hata Y, Takeuchi M, et al. (1997). "Binding of neuroligins to PSD-95.". Science 277 (5331): 1511–5. PMID 9278515.
Niethammer M, Valtschanoff JG, Kapoor TM, et al. (1998). "CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90.". Neuron 20 (4): 693–707. PMID 9581762.
Leonard AS, Davare MA, Horne MC, et al. (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. 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. PMID 9753324.
Brenman JE, Topinka JR, Cooper EC, et al. (1998). "Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A.". J. Neurosci. 18 (21): 8805–13. PMID 9786987.
Stathakis DG, Lee D, Bryant PJ (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.
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. PMID 10197530.
Sans N, Petralia RS, Wang YX, et al. (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. PMID 10725395.
Husi H, Ward MA, Choudhary JS, et al. (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. PMID 11095503.
Haraguchi K, Satoh K, Yanai H, et al. (2001). "The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase.". Genes Cells 5 (11): 905–911. 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. PMID 11771761.
Inanobe A, Fujita A, Ito M, et al. (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.