AKAP13

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A kinase (PRKA) anchor protein 13
Identifiers
Symbol(s) AKAP13; AKAP-Lbc; BRX; FLJ11952; FLJ43341; HA-3; Ht31; LBC; PROTO-LB; PROTO-LBC; c-lbc
External IDs OMIM: 604686 MGI2676556 Homologene4903
Orthologs
Human Mouse
Entrez 11214 75547
Ensembl ENSG00000170776 ENSMUSG00000066406
Uniprot Q12802 na
Refseq NM_006738 (mRNA)
NP_006729 (protein)
XM_133543 (mRNA)
XP_133543 (protein)
Location Chr 15: 83.58 - 84.09 Mb Chr 7: 75.33 - 75.61 Mb
Pubmed search [1] [2]

A kinase (PRKA) anchor protein 13, also known as AKAP13, is a human gene.[1]


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. Alternative splicing of this gene results in at least 3 transcript variants encoding different isoforms containing a dbl oncogene homology (DH) domain and a pleckstrin homology (PH) domain. The DH domain is associated with guanine nucleotide exchange activation for the Rho/Rac family of small GTP binding proteins, resulting in the conversion of the inactive GTPase to the active form capable of transducing signals. The PH domain has multiple functions. Therefore, these isoforms function as scaffolding proteins to coordinate a Rho signaling pathway and, in addition, function as protein kinase A-anchoring proteins.[1]


References

Further reading

  • Carr DW, Hausken ZE, Fraser ID; et al. (1992). "Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain.". J. Biol. Chem. 267 (19): 13376–82. PMID 1618839. 
  • Carr DW, Stofko-Hahn RE, Fraser ID; et al. (1991). "Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif.". J. Biol. Chem. 266 (22): 14188–92. PMID 1860836. 
  • Hausken ZE, Coghlan VM, Hastings CA; et al. (1994). "Type II regulatory subunit (RII) of the cAMP-dependent protein kinase interaction with A-kinase anchor proteins requires isoleucines 3 and 5.". J. Biol. Chem. 269 (39): 24245–51. PMID 7929081. 
  • Toksoz D, Williams DA (1994). "Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products.". Oncogene. 9 (2): 621–8. PMID 8290273. 
  • Rubino D, Driggers P, Arbit D; et al. (1998). "Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action.". Oncogene. 16 (19): 2513–26. PMID 9627117. doi:10.1038/sj.onc.1201783. 
  • Sterpetti P, Hack AA, Bashar MP; et al. (1999). "Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting.". Mol. Cell. Biol. 19 (2): 1334–45. PMID 9891067. 
  • Sagi SA, Seasholtz TM, Kobiashvili M; et al. (2001). "Physical and functional interactions of Galphaq with Rho and its exchange factors.". J. Biol. Chem. 276 (18): 15445–52. PMID 11278452. doi:10.1074/jbc.M008961200. 
  • Newlon MG, Roy M, Morikis D; et al. (2001). "A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes.". EMBO J. 20 (7): 1651–62. PMID 11285229. doi:10.1093/emboj/20.7.1651. 
  • Diviani D, Soderling J, Scott JD (2001). "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation.". J. Biol. Chem. 276 (47): 44247–57. PMID 11546812. doi:10.1074/jbc.M106629200. 
  • Driggers PH, Segars JH, Rubino DM (2002). "The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway.". J. Biol. Chem. 276 (50): 46792–7. PMID 11579095. doi:10.1074/jbc.M106927200. 
  • Klussmann E, Edemir B, Pepperle B; et al. (2001). "Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling.". FEBS Lett. 507 (3): 264–8. PMID 11696353. 
  • Park B, Nguyen NT, Dutt P; et al. (2003). "Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports serum response factor activation.". J. Biol. Chem. 277 (47): 45361–70. PMID 12270917. doi:10.1074/jbc.M202447200. 
  • Tan YC, Wu H, Wang WN; et al. (2003). "Characterization of the interactions between the small GTPase RhoA and its guanine nucleotide exchange factors.". Anal. Biochem. 310 (2): 156–62. PMID 12423633. 
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "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. PMID 12477932. doi:10.1073/pnas.242603899. 
  • Spierings E, Brickner AG, Caldwell JA; et al. (2003). "The minor histocompatibility antigen HA-3 arises from differential proteasome-mediated cleavage of the lymphoid blast crisis (Lbc) oncoprotein.". Blood. 102 (2): 621–9. PMID 12663445. doi:10.1182/blood-2003-01-0260. 
  • Alto NM, Soderling SH, Hoshi N; et al. (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. PMID 12672969. doi:10.1073/pnas.0330734100. 
  • Hornemann T, Kempa S, Himmel M; et al. (2003). "Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein.". J. Mol. Biol. 332 (4): 877–87. PMID 12972258. 
  • Dutt P, Nguyen N, Toksoz D (2004). "Role of Lbc RhoGEF in Galpha12/13-induced signals to Rho GTPase.". Cell. Signal. 16 (2): 201–9. PMID 14636890. 
  • Chen LY, Zuraw BL, Ye RD, Pan ZK (2004). "A Rho exchange factor mediates fMet-Leu-Phe-induced NF-kappaB activation in human peripheral blood monocytes.". J. Biol. Chem. 279 (8): 7208–12. PMID 14660653. doi:10.1074/jbc.M309542200. 
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. PMID 14702039. doi:10.1038/ng1285. 
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