DLGAP1

Discs, large (Drosophila) homolog-associated protein 1
Identifiers
Symbols	DLGAP1; DAP-1; DAP-1-ALPHA; DAP-1-BETA; FLJ38442; GKAP; MGC88156; SAPAP1; hGKAP
External IDs	OMIM: 605445 MGI: 1346065 HomoloGene: 31258 GeneCards: DLGAP1 Gene
Gene Ontology Molecular function • protein binding • protein domain specific binding Cellular component • cellular_component • plasma membrane • postsynaptic density • cell junction • synapse • postsynaptic membrane Biological process • synaptic transmission Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9229	224997
Ensembl	ENSG00000170579	ENSMUSG00000003279
UniProt	O14490	Q3TSN1
RefSeq (mRNA)	NM_001003809.2	NM_027712
RefSeq (protein)	NP_001003809.1	NP_081988
Location (UCSC)	Chr 18: 3.5 – 4.15 Mb	Chr 17: 70.32 – 71.17 Mb
PubMed search	[1]	[2]

Disks large-associated protein 1 (DAP-1), also known as guanylate kinase-associated protein (GKAP) is a protein that in humans is encoded by the DLGAP1 gene. DAP-1 is known to be highly enriched in synaptosomal preparations of the brain, and present in the post synaptic density^[1] This gene encodes the protein called guanylate kinase-associated protein (GKAP). GKAP binds to the SHANK and PSD-95 proteins fascilitating the assembly of the post synaptic density of neurons.^[2] Dlgap1 has five 14-amino acid repeats and three Pro-rich portions.

Interactions

DLGAP1 has been shown to interact with DLG4,^{[3][4][5][6][7][8]} DLG1,^[4][5][7][8] DYNLL2,^[3] SHANK2^[3][6] and DYNLL1.^[3].

The interaction with PSD95 and S-SCAM is mediated by the GUK domain^[9] and it has been hypothesized that this might mean it can also interact with other GUK containing proteins.

References

1. ^ "Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9229. 
2. ^ Hines RM, El-Husseini A (2006). "Mechanisms that regulate neuronal protein clustering at the synapse". In El-Husseini A, Dityatev A. Molecular mechanisms of synaptogenesis. Berlin: Springer. pp. 72–75. ISBN 0-387-32560-3. 
3. ^ ^{a b c d} Naisbitt, S; Valtschanoff J, Allison D W, Sala C, Kim E, Craig A M, Weinberg R J, Sheng M (Jun. 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". J. Neurosci. (UNITED STATES) 20 (12): 4524–34. ISSN 0270-6474. PMID 10844022. 
4. ^ ^{a b} Takeuchi, M; Hata Y, Hirao K, Toyoda A, Irie M, Takai Y (May. 1997). "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density". J. Biol. Chem. (UNITED STATES) 272 (18): 11943–51. doi:10.1074/jbc.272.18.11943. ISSN 0021-9258. PMID 9115257. 
5. ^ ^{a b} Satoh, K; Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T (Jun. 1997). "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95". Genes Cells (ENGLAND) 2 (6): 415–24. doi:10.1046/j.1365-2443.1997.1310329.x. ISSN 1356-9597. PMID 9286858. 
6. ^ ^{a b} Boeckers, T M; Winter C, Smalla K H, Kreutz M R, Bockmann J, Seidenbecher C, Garner C C, Gundelfinger E D (Oct. 1999). "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family". Biochem. Biophys. Res. Commun. (UNITED STATES) 264 (1): 247–52. doi:10.1006/bbrc.1999.1489. ISSN 0006-291X. PMID 10527873. 
7. ^ ^{a b} Wu, H; Reissner C, Kuhlendahl S, Coblentz B, Reuver S, Kindler S, Gundelfinger E D, Garner C C (Nov. 2000). "Intramolecular interactions regulate SAP97 binding to GKAP". EMBO J. (ENGLAND) 19 (21): 5740–51. doi:10.1093/emboj/19.21.5740. ISSN 0261-4189. PMC 305801. PMID 11060025. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=305801. 
8. ^ ^{a b} Kim, E; Naisbitt S, Hsueh Y P, Rao A, Rothschild A, Craig A M, Sheng M (Feb. 1997). "GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules". J. Cell Biol. (UNITED STATES) 136 (3): 669–78. doi:10.1083/jcb.136.3.669. ISSN 0021-9525. PMC 2134290. PMID 9024696. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2134290. 
9. ^ Hirao K, Hata Y, Ide N, Takeuchi M, Irie M, Yao I et al. (1998). "A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins.". J Biol Chem 273 (33): 21105–10. PMID 9694864. 

Further reading

• Kim E, Naisbitt S, Hsueh YP, et al. (1997). "GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules.". J. Cell Biol. 136 (3): 669–78. doi:10.1083/jcb.136.3.669. PMC 2134290. PMID 9024696. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2134290. 
• Takeuchi M, Hata Y, Hirao K, et al. (1997). "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density.". J. Biol. Chem. 272 (18): 11943–51. doi:10.1074/jbc.272.18.11943. PMID 9115257. 
• Naisbitt S, Kim E, Weinberg RJ, et al. (1997). "Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90.". J. Neurosci. 17 (15): 5687–96. PMID 9221768. 
• Satoh K, Yanai H, Senda T, et al. (1997). "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95.". Genes Cells 2 (6): 415–24. doi:10.1046/j.1365-2443.1997.1310329.x. PMID 9286858. 
• Hirao K, Hata Y, Ide N, et al. (1998). "A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins.". J. Biol. Chem. 273 (33): 21105–10. doi:10.1074/jbc.273.33.21105. PMID 9694864. 
• Deguchi M, Hata Y, Takeuchi M, et al. (1998). "BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein.". J. Biol. Chem. 273 (41): 26269–72. doi:10.1074/jbc.273.41.26269. PMID 9756850. 
• Kawabe H, Hata Y, Takeuchi M, et al. (1999). "nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP).". J. Biol. Chem. 274 (43): 30914–8. doi:10.1074/jbc.274.43.30914. PMID 10521485. 
• Boeckers TM, Winter C, Smalla KH, et al. (1999). "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family.". Biochem. Biophys. Res. Commun. 264 (1): 247–52. doi:10.1006/bbrc.1999.1489. PMID 10527873. 
• Naisbitt S, Valtschanoff J, Allison DW, et al. (2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein.". J. Neurosci. 20 (12): 4524–34. PMID 10844022. 
• Wu H, Reissner C, Kuhlendahl S, et al. (2000). "Intramolecular interactions regulate SAP97 binding to GKAP.". EMBO J. 19 (21): 5740–51. doi:10.1093/emboj/19.21.5740. PMC 305801. PMID 11060025. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=305801. 
• 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. doi:10.1046/j.1365-2443.2000.00374.x. PMID 11122378. 
• Lo KW, Naisbitt S, Fan JS, et al. (2001). "The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif.". J. Biol. Chem. 276 (17): 14059–66. doi:10.1074/jbc.M010320200. PMID 11148209. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Im YJ, Lee JH, Park SH, et al. (2004). "Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization.". J. Biol. Chem. 278 (48): 48099–104. doi:10.1074/jbc.M306919200. PMID 12954649. 
• Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain.". Mol. Cell Proteomics 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747. 
• Suzuki T, Li W, Zhang JP, et al. (2005). "A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins.". Eur. J. Neurosci. 21 (2): 339–50. doi:10.1111/j.1460-9568.2005.03856.x. PMID 15673434. 
• Sabio G, Arthur JS, Kuma Y, et al. (2005). "p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP.". EMBO J. 24 (6): 1134–45. doi:10.1038/sj.emboj.7600578. PMC 556394. PMID 15729360. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=556394.