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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''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]].<ref name="entrez">{{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 = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Discs, large (Drosophila) homolog-associated protein 1
| HGNCid = 2905
| Symbol = DLGAP1
| AltSymbols =; DAP-1; DAP-1-ALPHA; DAP-1-BETA; GKAP; MGC88156; SAPAP1; hGKAP
| OMIM = 605445
| ECnumber = 
| Homologene = 31258
| MGIid = 1346065
| GeneAtlas_image1 = PBB_GE_DLGAP1_206489_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DLGAP1_210750_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9229
    | Hs_Ensembl = ENSG00000170579
    | Hs_RefseqProtein = NP_001003809
    | Hs_RefseqmRNA = NM_001003809
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 18
    | Hs_GenLoc_start = 3488837
    | Hs_GenLoc_end = 3870135
    | Hs_Uniprot = O14490
    | Mm_EntrezGene = 224997
    | Mm_Ensembl = ENSMUSG00000003279
    | Mm_RefseqmRNA = NM_027712
    | Mm_RefseqProtein = NP_081988
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 70420924
    | Mm_GenLoc_end = 70723091
    | Mm_Uniprot = Q3TSN1
  }}
}}
'''Discs, large (Drosophila) homolog-associated protein 1''', also known as '''DLGAP1''' is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9229| accessdate = }}</ref>  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..<ref>"Molecular Mechanisms of Synaptogenesis." Edited by Alexander Dityatev and Alaa El-Husseini. Springer: New York, NY. 2006. pg. 72-75</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
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.<ref name="isbn0-387-32560-3">{{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 = 0-387-32560-3 | pages = 72–75 }}</ref> Dlgap1 has five 14-amino-acid repeats and three Pro-rich portions.
{{PBB_Summary
 
| section_title =  
== Interactions ==
| summary_text =  
 
}}
DLGAP1 has been shown to [[Protein-protein interaction|interact]] with:
* [[DLG1]],<ref name = pmid9115257/><ref name = pmid9286858/><ref name = pmid11060025/><ref name = pmid9024696/>
* [[DLG4]],<ref name = pmid9115257>{{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}}</ref><ref name = pmid9286858>{{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}}</ref><ref name = pmid11060025>{{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}}</ref><ref name = pmid9024696>{{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}}</ref><ref name = pmid10844022>{{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 = }}</ref><ref name = pmid10527873>{{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}}</ref>  
* [[DYNLL1]],<ref name = pmid10844022/>
* [[DYNLL2]],<ref name = pmid10844022/>  and
* [[SHANK2]]<ref name = pmid10844022/><ref name = pmid10527873/> and
 
The interaction with PSD95 and S-SCAM is mediated by the GUK domain<ref name="pmid9694864">{{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}}</ref> and it has been hypothesized that this might mean it can also interact with other GUK containing proteins.


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{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}}
| citations =
*{{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  | author=Kim E, Naisbitt S, Hsueh YP, ''et al.'' |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=  }}
*{{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=  |display-authors=etal}}
*{{cite journal  | author=Takeuchi M, Hata Y, Hirao K, ''et al.'' |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=  }}
*{{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  | author=Naisbitt S, Kim E, Weinberg RJ, ''et al.'' |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=  }}
*{{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  | author=Satoh K, Yanai H, Senda T, ''et al.'' |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=  }}
*{{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  | author=Hirao K, Hata Y, Ide N, ''et al.'' |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= }}
*{{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  | author=Deguchi M, Hata Y, Takeuchi M, ''et al.'' |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= }}
*{{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  | author=Kawabe H, Hata Y, Takeuchi M, ''et al.'' |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= }}
*{{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=  |display-authors=etal}}
*{{cite journal  | author=Boeckers TM, Winter C, Smalla KH, ''et al.'' |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 }}
*{{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  | author=Naisbitt S, Valtschanoff J, Allison DW, ''et al.'' |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=  }}
*{{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  | author=Wu H, Reissner C, Kuhlendahl S, ''et al.'' |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 }}
*{{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  | author=Haraguchi K, Satoh K, Yanai H, ''et al.'' |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=  }}
*{{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  | author=Lo KW, Naisbitt S, Fan JS, ''et al.'' |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 }}
*{{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  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{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  | author=Im YJ, Lee JH, Park SH, ''et al.'' |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 }}
*{{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  | author=Ballif BA, Villén J, Beausoleil SA, ''et al.'' |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 }}
*{{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}}
*{{cite journal  | author=Suzuki T, Li W, Zhang JP, ''et al.'' |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 }}
*{{cite journal  | author=Sabio G, Arthur JS, Kuma Y, ''et al.'' |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 }}
}}
{{refend}}
{{refend}}


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Revision as of 18:31, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
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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:

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".
  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. ↑ 3.0 3.1 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. 272 (18): 11943–51. doi:10.1074/jbc.272.18.11943. PMID 9115257.
  4. ↑ 4.0 4.1 Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T (June 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.
  5. ↑ 5.0 5.1 Wu H, Reissner C, Kuhlendahl S, Coblentz B, Reuver S, Kindler S, Gundelfinger ED, Garner CC (November 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.
  6. ↑ 6.0 6.1 Kim E, Naisbitt S, Hsueh YP, Rao A, Rothschild A, Craig AM, Sheng M (February 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.
  7. ↑ 7.0 7.1 7.2 7.3 Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M (June 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.
  8. ↑ 8.0 8.1 Boeckers TM, Winter C, Smalla KH, Kreutz MR, Bockmann J, Seidenbecher C, Garner CC, Gundelfinger ED (October 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.
  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. doi:10.1074/jbc.273.33.21105. PMID 9694864.

Further reading


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