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AKAP13
Introduction
A-kinase anchor protein 13 is an enzyme that in humans is encoded by the AKAP13 gene.[1][2][3]
Function
Function
The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins that 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.[3]
Interactions
Interactions
AKAP13 has been shown to interact with Estrogen receptor alpha,[1] CTNNAL1[4] and PRKAR2A.[5][6]
References
References
- ↑ 1.0 1.1 Rubino D, Driggers P, Arbit D, Kemp L, Miller B, Coso O, Pagliai K, Gray K, Gutkind S, Segars J (Jul 1998). “Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action”. Oncogene. 16 (19): 2513–26. doi:10.1038/sj.onc.1201783. PMID 9627117.
- ↑ Carr DW, Stofko-Hahn RE, Fraser ID, Bishop SM, Acott TS, Brennan RG, Scott JD (Sep 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.
- ↑ 3.0 3.1 “Entrez Gene: AKAP13 A kinase (PRKA) anchor protein 13”.
- ↑ Park B, Nguyen NT, Dutt P, Merdek KD, Bashar M, Sterpetti P, Tosolini A, Testa JR, Toksoz D (Nov 2002). “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. doi:10.1074/jbc.M202447200. PMID 12270917.
- ↑ 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.
- ↑ Carr DW, Hausken ZE, Fraser ID, Stofko-Hahn RE, Scott JD (Jul 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.
External links
External links
- Human AKAP13 genome location and AKAP13 gene details page in the UCSC Genome Browser.
Further reading
Further reading
- Carr DW, Hausken ZE, Fraser ID, Stofko-Hahn RE, Scott JD (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.
- Hausken ZE, Coghlan VM, Hastings CA, Reimann EM, Scott JD (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.
- Sterpetti P, Hack AA, Bashar MP, Park B, Cheng SD, Knoll JH, Urano T, Feig LA, Toksoz D (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. PMC 116062. PMID 9891067.
- Sagi SA, Seasholtz TM, Kobiashvili M, Wilson BA, Toksoz D, Brown JH (2001). “Physical and functional interactions of Galphaq with Rho and its exchange factors”. J. Biol. Chem. 276 (18): 15445–52. doi:10.1074/jbc.M008961200. PMC 1761691. PMID 11278452.
- Newlon MG, Roy M, Morikis D, Carr DW, Westphal R, Scott JD, Jennings PA (2001). “A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes”. EMBO J. 20 (7): 1651–62. doi:10.1093/emboj/20.7.1651. PMC 145475. PMID 11285229.
- 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. doi:10.1074/jbc.M106629200. PMID 11546812.
- Driggers PH, Segars JH, Rubino DM (2001). “The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway”. J. Biol. Chem. 276 (50): 46792–7. doi:10.1074/jbc.M106927200. PMC 4152864. PMID 11579095.
- Klussmann E, Edemir B, Pepperle B, Tamma G, Henn V, Klauschenz E, Hundsrucker C, Maric K, Rosenthal W (2001). “Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling”. FEBS Lett. 507 (3): 264–8. doi:10.1016/S0014-5793(01)02995-7. PMID 11696353.
- Park B, Nguyen NT, Dutt P, Merdek KD, Bashar M, Sterpetti P, Tosolini A, Testa JR, Toksoz D (2002). “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. doi:10.1074/jbc.M202447200. PMID 12270917.
- Tan YC, Wu H, Wang WN, Zheng Y, Wang ZX (2002). “Characterization of the interactions between the small GTPase RhoA and its guanine nucleotide exchange factors”. Anal. Biochem. 310 (2): 156–62. doi:10.1016/S0003-2697(02)00382-2. PMID 12423633.
- Spierings E, Brickner AG, Caldwell JA, Zegveld S, Tatsis N, Blokland E, Pool J, Pierce RA, Mollah S, Shabanowitz J, Eisenlohr LC, van Veelen P, Ossendorp F, Hunt DF, Goulmy E, Engelhard VH (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. doi:10.1182/blood-2003-01-0260. PMID 12663445.
- Alto NM, Soderling SH, Hoshi N, Langeberg LK, Fayos R, Jennings PA, Scott JD (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.
- Hornemann T, Kempa S, Himmel M, Hayess K, Fürst DO, Wallimann T (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. doi:10.1016/S0022-2836(03)00921-5. 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. doi:10.1016/S0898-6568(03)00132-3. 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. doi:10.1074/jbc.M309542200. PMID 14660653.