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词条 DLGAP1
释义

  1. Function

  2. Interactions

  3. References

  4. Further reading

{{Infobox_gene}}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 SHANK 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:

  • DLG1[3][4][5][6]
  • DLG4[3][4][5][6][7][8]
  • DYNLL1[7]
  • DYNLL2[7]
  • SHANK2[7][8]

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. ^{{cite web | title = Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9229| accessdate = }}
2. ^{{cite book | veditors = El-Husseini A, Dityatev A | title = Molecular mechanisms of synaptogenesis | publisher = Springer | location = Berlin | year = 2006 | chapter = Mechanisms that regulate neuronal protein clustering at the synapse| vauthors = Hines RM, El-Husseini A | isbn = 978-0-387-32560-6 | pages = 72–75 }}
3. ^1 {{cite journal | date = May 1997 | vauthors = Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y | title = SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density | journal = J. Biol. Chem. | volume = 272 | issue = 18 | pages = 11943–51 | pmid = 9115257 | doi = 10.1074/jbc.272.18.11943}}
4. ^1 {{cite journal | date = June 1997 | vauthors = Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T | title = DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95 | journal = Genes Cells | volume = 2 | issue = 6 | pages = 415–24 | pmid = 9286858 | doi = 10.1046/j.1365-2443.1997.1310329.x}}
5. ^1 {{cite journal | date = November 2000 | vauthors = Wu H, Reissner C, Kuhlendahl S, Coblentz B, Reuver S, Kindler S, Gundelfinger ED, Garner CC | title = Intramolecular interactions regulate SAP97 binding to GKAP | journal = EMBO J. | volume = 19 | issue = 21 | pages = 5740–51 | pmid = 11060025 | pmc = 305801 | doi = 10.1093/emboj/19.21.5740}}
6. ^1 {{cite journal | date = February 1997 | vauthors = Kim E, Naisbitt S, Hsueh YP, Rao A, Rothschild A, Craig AM, Sheng M | title = GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules | journal = J. Cell Biol. | volume = 136 | issue = 3 | pages = 669–78 | pmid = 9024696 | pmc = 2134290 | doi = 10.1083/jcb.136.3.669}}
7. ^1 2 3 {{cite journal | date = June 2000 | vauthors = Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M | title = Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein | journal = J. Neurosci. | volume = 20 | issue = 12 | pages = 4524–34 | pmid = 10844022 | doi = 10.1523/JNEUROSCI.20-12-04524.2000}}
8. ^1 {{cite journal | date = October 1999 | vauthors = Boeckers TM, Winter C, Smalla KH, Kreutz MR, Bockmann J, Seidenbecher C, Garner CC, Gundelfinger ED | title = Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family | journal = Biochem. Biophys. Res. Commun. | volume = 264 | issue = 1 | pages = 247–52 | pmid = 10527873 | doi = 10.1006/bbrc.1999.1489}}
9. ^{{cite journal| vauthors=Hirao K, Hata Y, Ide N, Takeuchi M, Irie M, Yao I| title=A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins. | journal=J Biol Chem | year= 1998 | volume= 273 | issue= 33 | pages= 21105–10 | pmid=9694864 | doi= 10.1074/jbc.273.33.21105| pmc= | url= |display-authors=etal}}

Further reading

{{refbegin | 2}}
  • {{cite journal | vauthors=Kim E, Naisbitt S, Hsueh YP |title=GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules. |journal=J. Cell Biol. |volume=136 |issue= 3 |pages= 669–78 |year= 1997 |pmid= 9024696 |doi=10.1083/jcb.136.3.669 | pmc=2134290 |display-authors=etal}}
  • {{cite journal | vauthors=Takeuchi M, Hata Y, Hirao K |title=SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 11943–51 |year= 1997 |pmid= 9115257 |doi=10.1074/jbc.272.18.11943 |display-authors=etal}}
  • {{cite journal | vauthors=Naisbitt S, Kim E, Weinberg RJ |title=Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90. |journal=J. Neurosci. |volume=17 |issue= 15 |pages= 5687–96 |year= 1997 |pmid= 9221768 |doi= 10.1523/JNEUROSCI.17-15-05687.1997|display-authors=etal}}
  • {{cite journal | vauthors=Satoh K, Yanai H, Senda T |title=DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95. |journal=Genes Cells |volume=2 |issue= 6 |pages= 415–24 |year= 1997 |pmid= 9286858 |doi=10.1046/j.1365-2443.1997.1310329.x |display-authors=etal}}
  • {{cite journal | vauthors=Hirao K, Hata Y, Ide N |title=A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins. |journal=J. Biol. Chem. |volume=273 |issue= 33 |pages= 21105–10 |year= 1998 |pmid= 9694864 |doi=10.1074/jbc.273.33.21105 |display-authors=etal}}
  • {{cite journal | vauthors=Deguchi M, Hata Y, Takeuchi M |title=BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein. |journal=J. Biol. Chem. |volume=273 |issue= 41 |pages= 26269–72 |year= 1998 |pmid= 9756850 |doi=10.1074/jbc.273.41.26269 |display-authors=etal}}
  • {{cite journal | vauthors=Kawabe H, Hata Y, Takeuchi M |title=nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP). |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30914–8 |year= 1999 |pmid= 10521485 |doi=10.1074/jbc.274.43.30914 |display-authors=etal}}
  • {{cite journal | vauthors=Boeckers TM, Winter C, Smalla KH |title=Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family. |journal=Biochem. Biophys. Res. Commun. |volume=264 |issue= 1 |pages= 247–52 |year= 1999 |pmid= 10527873 |doi= 10.1006/bbrc.1999.1489 |display-authors=etal}}
  • {{cite journal | vauthors=Naisbitt S, Valtschanoff J, Allison DW |title=Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. |journal=J. Neurosci. |volume=20 |issue= 12 |pages= 4524–34 |year= 2000 |pmid= 10844022 |doi= 10.1523/JNEUROSCI.20-12-04524.2000|display-authors=etal}}
  • {{cite journal | vauthors=Wu H, Reissner C, Kuhlendahl S |title=Intramolecular interactions regulate SAP97 binding to GKAP. |journal=EMBO J. |volume=19 |issue= 21 |pages= 5740–51 |year= 2000 |pmid= 11060025 |doi= 10.1093/emboj/19.21.5740 | pmc=305801 |display-authors=etal}}
  • {{cite journal | vauthors=Haraguchi K, Satoh K, Yanai H |title=The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase. |journal=Genes Cells |volume=5 |issue= 11 |pages= 905–911 |year= 2001 |pmid= 11122378 |doi=10.1046/j.1365-2443.2000.00374.x |display-authors=etal}}
  • {{cite journal | vauthors=Lo KW, Naisbitt S, Fan JS |title=The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 14059–66 |year= 2001 |pmid= 11148209 |doi= 10.1074/jbc.M010320200 |display-authors=etal}}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
  • {{cite journal | vauthors=Im YJ, Lee JH, Park SH |title=Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization. |journal=J. Biol. Chem. |volume=278 |issue= 48 |pages= 48099–104 |year= 2004 |pmid= 12954649 |doi= 10.1074/jbc.M306919200 |display-authors=etal}}
  • {{cite journal | vauthors=Ballif BA, Villén J, Beausoleil SA |title=Phosphoproteomic analysis of the developing mouse brain. |journal=Mol. Cell. Proteomics |volume=3 |issue= 11 |pages= 1093–101 |year= 2005 |pmid= 15345747 |doi= 10.1074/mcp.M400085-MCP200 |display-authors=etal}}
  • {{cite journal | vauthors=Suzuki T, Li W, Zhang JP |title=A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins. |journal=Eur. J. Neurosci. |volume=21 |issue= 2 |pages= 339–50 |year= 2005 |pmid= 15673434 |doi= 10.1111/j.1460-9568.2005.03856.x |display-authors=etal}}
  • {{cite journal | vauthors=Sabio G, Arthur JS, Kuma Y |title=p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP. |journal=EMBO J. |volume=24 |issue= 6 |pages= 1134–45 |year= 2005 |pmid= 15729360 |doi= 10.1038/sj.emboj.7600578 | pmc=556394 |display-authors=etal}}
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