DLGAP1

Discs, large (Drosophila) homolog-associated protein 1

Identifiers

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

RefSeq (mRNA)

RefSeq (protein)

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

^ "Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9229.
^ 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.
^ ^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.
^ ^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.
^ ^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.
^ ^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.
^ ^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.
^ ^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.
^ 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. doi:10.1074/jbc.273.33.21105. PMID 9694864.

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.

DLGAP1

Interactions

References

Further reading