AKAP9

A kinase (PRKA) anchor protein 9
Identifiers
Symbols AKAP9 ; AKAP-9; AKAP350; AKAP450; CG-NAP; HYPERION; LQT11; MU-RMS-40.16A; PPP1R45; PRKA9; YOTIAO
External IDs OMIM: 604001 MGI: 2178217 HomoloGene: 17517 GeneCards: AKAP9 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 10142 100986
Ensembl ENSG00000127914 ENSMUSG00000040407
UniProt Q99996 Q70FJ1
RefSeq (mRNA) NM_005751 NM_194462
RefSeq (protein) NP_005742 NP_919444
Location (UCSC) Chr 7:
91.94 – 92.11 Mb
Chr 5:
3.93 – 4.08 Mb
PubMed search

A-kinase anchor protein 9 is a protein that in humans is encoded by the AKAP9 gene.[1][2][3]

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[14][15] 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.[16][17][18]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][19] Twenty six tests were carried out on mutant mice and eight significant abnormalities were observed.[13] 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.[13]

Interactions

AKAP9 has been shown to interact with:

References

  1. Lin JW, Wyszynski M, Madhavan R, Sealock R, Kim JU, Sheng M (Apr 1998). "Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1". J Neurosci 18 (6): 2017–27. PMID 9482789.
  2. Westphal RS, Tavalin SJ, Lin JW, Alto NM, Fraser ID, Langeberg LK, Sheng M, Scott JD (Jul 1999). "Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex". Science 285 (5424): 93–6. doi:10.1126/science.285.5424.93. PMID 10390370.
  3. 1 2 "Entrez Gene: AKAP9 A kinase (PRKA) anchor protein (yotiao) 9".
  4. "Body weight data for Akap9". Wellcome Trust Sanger Institute.
  5. "Indirect calorimetry data for Akap9". Wellcome Trust Sanger Institute.
  6. "Glucose tolerance test data for Akap9". Wellcome Trust Sanger Institute.
  7. "DEXA data for Akap9". Wellcome Trust Sanger Institute.
  8. "Radiography data for Akap9". Wellcome Trust Sanger Institute.
  9. "Clinical chemistry data for Akap9". Wellcome Trust Sanger Institute.
  10. "Salmonella infection data for Akap9". Wellcome Trust Sanger Institute.
  11. "Citrobacter infection data for Akap9". Wellcome Trust Sanger Institute.
  12. Mouse Resources Portal, Wellcome Trust Sanger Institute.
  13. 1 2 3 4 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  14. "International Knockout Mouse Consortium".
  15. "Mouse Genome Informatics".
  16. 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 (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  17. Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  18. Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  19. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  20. 1 2 Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y (Sep 2002). "Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex". Mol. Biol. Cell 13 (9): 3235–45. doi:10.1091/mbc.E02-02-0112. PMC 124155. PMID 12221128.
  21. 1 2 Larocca MC, Shanks RA, Tian L, Nelson DL, Stewart DM, Goldenring JR (Jun 2004). "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus". Mol. Biol. Cell 15 (6): 2771–81. doi:10.1091/mbc.E03-10-0757. PMC 420101. PMID 15047863.
  22. Marx SO, Kurokawa J, Reiken S, Motoike H, D'Armiento J, Marks AR, Kass RS (Jan 2002). "Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel". Science 295 (5554): 496–9. doi:10.1126/science.1066843. PMID 11799244.
  23. 1 2 Takahashi M, Shibata H, Shimakawa M, Miyamoto M, Mukai H, Ono Y (Jun 1999). "Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus". J. Biol. Chem. 274 (24): 17267–74. doi:10.1074/jbc.274.24.17267. PMID 10358086.
  24. Alto NM, Soderling SH, Hoshi N, Langeberg LK, Fayos R, Jennings PA, Scott JD (Apr 2003). "Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein kinase A anchoring". Proc. Natl. Acad. Sci. U.S.A. 100 (8): 4445–50. doi:10.1073/pnas.0330734100. PMC 153575. PMID 12672969.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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