Biology:DLGAP1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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]
Function
This gene encodes the protein called guanylate kinase-associated protein (GKAP). GKAP binds to the SHANK2 and PSD-95 proteins, facilitating 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:
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". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9229.
- ↑ "Mechanisms that regulate neuronal protein clustering at the synapse". Molecular mechanisms of synaptogenesis. Berlin: Springer. 2006. pp. 72–75. ISBN 978-0-387-32560-6.
- ↑ 3.0 3.1 "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density". J. Biol. Chem. 272 (18): 11943–51. May 1997. doi:10.1074/jbc.272.18.11943. PMID 9115257.
- ↑ 4.0 4.1 "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95". Genes Cells 2 (6): 415–24. June 1997. doi:10.1046/j.1365-2443.1997.1310329.x. PMID 9286858.
- ↑ 5.0 5.1 "Intramolecular interactions regulate SAP97 binding to GKAP". EMBO J. 19 (21): 5740–51. November 2000. doi:10.1093/emboj/19.21.5740. PMID 11060025.
- ↑ 6.0 6.1 "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. February 1997. doi:10.1083/jcb.136.3.669. PMID 9024696.
- ↑ 7.0 7.1 7.2 7.3 "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. June 2000. doi:10.1523/JNEUROSCI.20-12-04524.2000. PMID 10844022.
- ↑ 8.0 8.1 "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. October 1999. doi:10.1006/bbrc.1999.1489. PMID 10527873.
- ↑ "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. 1998. doi:10.1074/jbc.273.33.21105. PMID 9694864.
Further reading
- "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. 1997. doi:10.1083/jcb.136.3.669. PMID 9024696.
- "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density.". J. Biol. Chem. 272 (18): 11943–51. 1997. doi:10.1074/jbc.272.18.11943. PMID 9115257.
- "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. 1997. doi:10.1523/JNEUROSCI.17-15-05687.1997. PMID 9221768.
- "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95.". Genes Cells 2 (6): 415–24. 1997. doi:10.1046/j.1365-2443.1997.1310329.x. PMID 9286858.
- "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. 1998. doi:10.1074/jbc.273.33.21105. PMID 9694864.
- "BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein.". J. Biol. Chem. 273 (41): 26269–72. 1998. doi:10.1074/jbc.273.41.26269. PMID 9756850.
- "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. 1999. doi:10.1074/jbc.274.43.30914. PMID 10521485.
- "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. 1999. doi:10.1006/bbrc.1999.1489. PMID 10527873.
- "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. 2000. doi:10.1523/JNEUROSCI.20-12-04524.2000. PMID 10844022.
- "Intramolecular interactions regulate SAP97 binding to GKAP.". EMBO J. 19 (21): 5740–51. 2000. doi:10.1093/emboj/19.21.5740. PMID 11060025.
- "The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase.". Genes Cells 5 (11): 905–911. 2001. doi:10.1046/j.1365-2443.2000.00374.x. PMID 11122378.
- "The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif.". J. Biol. Chem. 276 (17): 14059–66. 2001. doi:10.1074/jbc.M010320200. PMID 11148209.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "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. 2004. doi:10.1074/jbc.M306919200. PMID 12954649.
- "Phosphoproteomic analysis of the developing mouse brain.". Mol. Cell. Proteomics 3 (11): 1093–101. 2005. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
- "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. 2005. doi:10.1111/j.1460-9568.2005.03856.x. PMID 15673434.
- Sabio G 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. PMID 15729360.
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