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词条 AKAP9
释义

  1. Function

  2. Model organisms

  3. Interactions

  4. References

  5. Further reading

  6. External links

{{Infobox_gene}}A-kinase anchor protein 9 is a protein that in humans is encoded by the AKAP9 gene.[1][2][3] AKAP9 is also known as Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP) or AKAP350 or AKAP450 [4]

Function

The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. Alternate splicing of this gene results in many isoforms that localize to the centrosome and the Golgi apparatus, and interact with numerous signaling proteins from multiple signal transduction pathways. These signaling proteins include type II protein kinase A, serine/threonine kinase protein kinase N, protein phosphatase 1, protein phosphatase 2a, protein kinase C-epsilon and phosphodiesterase 4D3.[3]

Model organisms

Model organisms have been used in the study of AKAP9 function. A conditional knockout mouse line, called Akap9tm1a(KOMP)Wtsi[15][16] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[17][18][19]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[14][20] Twenty six tests were carried out on mutant mice and eight significant abnormalities were observed.[14] Fewer than expected homozygous mutant mice survived until weaning. The remaining tests were carried out on both homozygous and heterozygous mutant adult mice. Animals of both sex displayed decreased body fat and body weight, hematopoietic abnormalities and an atypical plasma chemistry panel. Female homozygotes also displayed abnormal tooth morphology while males heterozygous animals displayed an abnormal pelvic girdle bone morphology.[14]

Interactions

AKAP9 has been shown to interact with:

{{div col|colwidth=20em}}
  • CALM2,[25]
  • CALM1,[21]
  • FNBP1,[22]
  • KvLQT1[23]
  • PRKAR2A,[29][24]
  • PKN1,[25] and
  • TRIP10.[22]
{{Div col end}}{{clear}}

References

1. ^{{cite journal | vauthors = Lin JW, Wyszynski M, Madhavan R, Sealock R, Kim JU, Sheng M | title = Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1 | journal = J Neurosci | volume = 18 | issue = 6 | pages = 2017–27 | date = Apr 1998 | pmid = 9482789 | pmc = | doi = }}
2. ^{{cite journal | vauthors = Westphal RS, Tavalin SJ, Lin JW, Alto NM, Fraser ID, Langeberg LK, Sheng M, Scott JD | title = Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex | journal = Science | volume = 285 | issue = 5424 | pages = 93–6 | date = Jul 1999 | pmid = 10390370 | pmc = | doi = 10.1126/science.285.5424.93 }}
3. ^{{cite web | title = Entrez Gene: AKAP9 A kinase (PRKA) anchor protein (yotiao) 9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10142| accessdate = }}
4. ^{{cite journal | vauthors = Ong ST, Chalasani ML, Fazil MH, Prasannan P, Kizhakeyil A, Wright GD, Kelleher D, Verma NK | title = Centrosome- and Golgi-Localized Protein Kinase N-Associated Protein Serves As a Docking Platform for Protein Kinase A Signaling and Microtubule Nucleation in Migrating T-Cells | journal = Front. Immunol. | volume = 9 | issue = 397 | pages = 397| date = Mar 2018 | pmid = 29545805 | pmc = 5837996 | doi = 10.3389/fimmu.2018.00397 }}
5. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/weight-curves/ |title=Body weight data for Akap9 |publisher=Wellcome Trust Sanger Institute}}
6. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/indirect-calorimetry/ |title=Indirect calorimetry data for Akap9 |publisher=Wellcome Trust Sanger Institute}}
7. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/glucose-tolerance-ip/ |title=Glucose tolerance test data for Akap9 |publisher=Wellcome Trust Sanger Institute}}
8. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/body-composition-dexa/ |title=DEXA data for Akap9 |publisher=Wellcome Trust Sanger Institute}}
9. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/x-ray-imaging/ |title=Radiography data for Akap9 |publisher=Wellcome Trust Sanger Institute}}
10. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/plasma-chemistry/ |title=Clinical chemistry data for Akap9 |publisher=Wellcome Trust Sanger Institute}}
11. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/salmonella-challenge/ |title=Salmonella infection data for Akap9 |publisher=Wellcome Trust Sanger Institute}}
12. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/citrobacter-challenge/ |title=Citrobacter infection data for Akap9 |publisher=Wellcome Trust Sanger Institute}}
13. ^Mouse Resources Portal, Wellcome Trust Sanger Institute.
14. ^{{cite journal | doi = 10.1111/j.1755-3768.2010.4142.x | title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice | year = 2010 | author = Gerdin AK | journal = Acta Ophthalmologica | volume = 88 | pages = 925–7 }}
15. ^{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Akap9 |title=International Knockout Mouse Consortium}}
16. ^{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4362642 |title=Mouse Genome Informatics}}
17. ^{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–342 | year = 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}
18. ^{{cite journal | author = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | year = 2011 | pmid = 21677718 | doi = 10.1038/474262a }}
19. ^{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A Mouse for All Reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | year = 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}
20. ^{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism. | journal = Genome Biol | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}
21. ^{{cite journal | vauthors = Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y | title = Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex | journal = Mol. Biol. Cell | volume = 13 | issue = 9 | pages = 3235–45 | date = Sep 2002 | pmid = 12221128 | pmc = 124155 | doi = 10.1091/mbc.E02-02-0112 }}
22. ^{{cite journal | vauthors = Larocca MC, Shanks RA, Tian L, Nelson DL, Stewart DM, Goldenring JR | title = AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus | journal = Mol. Biol. Cell | volume = 15 | issue = 6 | pages = 2771–81 | date = Jun 2004 | pmid = 15047863 | pmc = 420101 | doi = 10.1091/mbc.E03-10-0757 }}
23. ^{{cite journal | vauthors = Marx SO, Kurokawa J, Reiken S, Motoike H, D'Armiento J, Marks AR, Kass RS | title = Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel | journal = Science | volume = 295 | issue = 5554 | pages = 496–9 | date = Jan 2002 | pmid = 11799244 | doi = 10.1126/science.1066843 }}
24. ^{{cite journal | vauthors = Alto NM, Soderling SH, Hoshi N, Langeberg LK, Fayos R, Jennings PA, Scott JD | title = Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein kinase A anchoring | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 100 | issue = 8 | pages = 4445–50 | date = Apr 2003 | pmid = 12672969 | pmc = 153575 | doi = 10.1073/pnas.0330734100 }}
25. ^{{cite journal | vauthors = Takahashi M, Shibata H, Shimakawa M, Miyamoto M, Mukai H, Ono Y | title = Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus | journal = J. Biol. Chem. | volume = 274 | issue = 24 | pages = 17267–74 | date = Jun 1999 | pmid = 10358086 | doi = 10.1074/jbc.274.24.17267 }}

Further reading

{{refbegin|35em}}
  • {{cite journal | vauthors = Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Res. | volume = 5 | issue = 5 | pages = 277–86 | year = 1999 | pmid = 9872452 | doi = 10.1093/dnares/5.5.277 }}
  • {{cite journal | vauthors = Schmidt PH, Dransfield DT, Claudio JO, Hawley RG, Trotter KW, Milgram SL, Goldenring JR | title = AKAP350, a multiply spliced protein kinase A-anchoring protein associated with centrosomes | journal = J. Biol. Chem. | volume = 274 | issue = 5 | pages = 3055–66 | year = 1999 | pmid = 9915845 | doi = 10.1074/jbc.274.5.3055 }}
  • {{cite journal | vauthors = Witczak O, Skålhegg BS, Keryer G, Bornens M, Taskén K, Jahnsen T, Orstavik S | title = Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450 | journal = EMBO J. | volume = 18 | issue = 7 | pages = 1858–68 | year = 1999 | pmid = 10202149 | pmc = 1171271 | doi = 10.1093/emboj/18.7.1858 }}
  • {{cite journal | vauthors = Takahashi M, Shibata H, Shimakawa M, Miyamoto M, Mukai H, Ono Y | title = Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus | journal = J. Biol. Chem. | volume = 274 | issue = 24 | pages = 17267–74 | year = 1999 | pmid = 10358086 | doi = 10.1074/jbc.274.24.17267 }}
  • {{cite journal | vauthors = Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG | title = Proteomic analysis of NMDA receptor-adhesion protein signaling complexes | journal = Nat. Neurosci. | volume = 3 | issue = 7 | pages = 661–9 | year = 2000 | pmid = 10862698 | doi = 10.1038/76615 }}
  • {{cite journal | vauthors = Takahashi M, Mukai H, Oishi K, Isagawa T, Ono Y | title = Association of immature hypophosphorylated protein kinase cepsilon with an anchoring protein CG-NAP | journal = J. Biol. Chem. | volume = 275 | issue = 44 | pages = 34592–6 | year = 2000 | pmid = 10945988 | doi = 10.1074/jbc.M005285200 }}
  • {{cite journal | vauthors = Marx SO, Kurokawa J, Reiken S, Motoike H, D'Armiento J, Marks AR, Kass RS | title = Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel | journal = Science | volume = 295 | issue = 5554 | pages = 496–9 | year = 2002 | pmid = 11799244 | doi = 10.1126/science.1066843 }}
  • {{cite journal | vauthors = Steadman BT, Schmidt PH, Shanks RA, Lapierre LA, Goldenring JR | title = Transforming acidic coiled-coil-containing protein 4 interacts with centrosomal AKAP350 and the mitotic spindle apparatus | journal = J. Biol. Chem. | volume = 277 | issue = 33 | pages = 30165–76 | year = 2002 | pmid = 12015314 | doi = 10.1074/jbc.M201914200 }}
  • {{cite journal | vauthors = Bray JD, Chennathukuzhi VM, Hecht NB | title = Identification and characterization of cDNAs encoding four novel proteins that interact with translin associated factor-X | journal = Genomics | volume = 79 | issue = 6 | pages = 799–808 | year = 2002 | pmid = 12036294 | doi = 10.1006/geno.2002.6779 }}
  • {{cite journal | vauthors = Shanks RA, Larocca MC, Berryman M, Edwards JC, Urushidani T, Navarre J, Goldenring JR | title = AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel chloride intracellular channel (CLIC) family member | journal = J. Biol. Chem. | volume = 277 | issue = 43 | pages = 40973–80 | year = 2002 | pmid = 12163479 | doi = 10.1074/jbc.M112277200 }}
  • {{cite journal | vauthors = Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y | title = Centrosomal Proteins CG-NAP and Kendrin Provide Microtubule Nucleation Sites by Anchoring γ-Tubulin Ring Complex | journal = Mol. Biol. Cell | volume = 13 | issue = 9 | pages = 3235–45 | year = 2003 | pmid = 12221128 | pmc = 124155 | doi = 10.1091/mbc.E02-02-0112 }}
  • {{cite journal | vauthors = Sillibourne JE, Milne DM, Takahashi M, Ono Y, Meek DW | title = Centrosomal anchoring of the protein kinase CK1delta mediated by attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450 | journal = J. Mol. Biol. | volume = 322 | issue = 4 | pages = 785–97 | year = 2002 | pmid = 12270714 | doi = 10.1016/S0022-2836(02)00857-4 }}
  • {{cite journal | vauthors = Tu H, Tang TS, Wang Z, Bezprozvanny I | title = Association of type 1 inositol 1,4,5-trisphosphate receptor with AKAP9 (Yotiao) and protein kinase A | journal = J. Biol. Chem. | volume = 279 | issue = 18 | pages = 19375–82 | year = 2004 | pmid = 14982933 | doi = 10.1074/jbc.M313476200 }}
{{refend}}

External links

  • {{UCSC genome browser|AKAP9}}
  • {{UCSC gene details|AKAP9}}
{{NLM content}}

2 : Genes mutated in mice|A-kinase-anchoring proteins

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