A kinase anchor protein 1, mitochondrial is an enzyme that in humans is encoded by the AKAP1gene.[5][6][7]
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. The encoded protein binds to type I and type II regulatory subunits of PKA and anchors them to the mitochondrion. This protein is speculated to be involved in the cAMP-dependent signal transduction pathway and in directing RNA to a specific cellular compartment.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Trendelenburg G, Hummel M, Riecken EO, Hanski C (Sep 1996). "Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain". Biochem Biophys Res Commun. 225 (1): 313–9. doi:10.1006/bbrc.1996.1172. PMID8769136.
^Lin RY, Moss SB, Rubin CS (Jan 1996). "Characterization of S-AKAP84, a novel developmentally regulated A kinase anchor protein of male germ cells". J Biol Chem. 270 (46): 27804–11. doi:10.1074/jbc.270.46.27804. PMID7499250.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ abYukitake H, Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H (Nov 2002). "AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary complex with AMY-1, A-kinase anchor protein 84, and a regulatory subunit of cAMP-dependent protein kinase and is phosphorylated by its kinase". J. Biol. Chem. 277 (47): 45480–92. doi:10.1074/jbc.M206201200. PMID12223483.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^Furusawa M, Ohnishi T, Taira T, Iguchi-Ariga SM, Ariga H (Sep 2001). "AMY-1, a c-Myc-binding protein, is localized in the mitochondria of sperm by association with S-AKAP84, an anchor protein of cAMP-dependent protein kinase". J. Biol. Chem. 276 (39): 36647–51. doi:10.1074/jbc.M103885200. PMID11483602.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ abCarlson CR, Ruppelt A, Taskén K (Mar 2003). "A kinase anchoring protein (AKAP) interaction and dimerization of the RIalpha and RIbeta regulatory subunits of protein kinase a in vivo by the yeast two hybrid system". J. Mol. Biol. 327 (3): 609–18. doi:10.1016/S0022-2836(03)00093-7. PMID12634056.
^ abHerberg FW, Maleszka A, Eide T, Vossebein L, Tasken K (April 2000). "Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding". J. Mol. Biol. 298 (2): 329–39. doi:10.1006/jmbi.2000.3662. PMID10764601.
^Kapiloff MS, Schillace RV, Westphal AM, Scott JD (Aug 1999). "mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes". J. Cell Sci. 112 (16): 2725–36. PMID10413680.
Huang LJ, Durick K, Weiner JA, et al. (1997). "Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits". J. Biol. Chem. 272 (12): 8057–64. doi:10.1074/jbc.272.12.8057. PMID9065479.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Herberg FW, Maleszka A, Eide T, et al. (2000). "Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding". J. Mol. Biol. 298 (2): 329–39. doi:10.1006/jmbi.2000.3662. PMID10764601.
Furusawa M, Ohnishi T, Taira T, et al. (2001). "AMY-1, a c-Myc-binding protein, is localized in the mitochondria of sperm by association with S-AKAP84, an anchor protein of cAMP-dependent protein kinase". J. Biol. Chem. 276 (39): 36647–51. doi:10.1074/jbc.M103885200. PMID11483602.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Razani B, Lisanti MP (2001). "Two distinct caveolin-1 domains mediate the functional interaction of caveolin-1 with protein kinase A". Am. J. Physiol., Cell Physiol. 281 (4): C1241–50. PMID11546661.
Yukitake H, Furusawa M, Taira T, et al. (2003). "AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary complex with AMY-1, A-kinase anchor protein 84, and a regulatory subunit of cAMP-dependent protein kinase and is phosphorylated by its kinase". J. Biol. Chem. 277 (47): 45480–92. doi:10.1074/jbc.M206201200. PMID12223483.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H (2003). "AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex". J. Biol. Chem. 277 (52): 50885–92. doi:10.1074/jbc.M206387200. PMID12414807.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Carlson CR, Ruppelt A, Taskén K (2003). "A kinase anchoring protein (AKAP) interaction and dimerization of the RIalpha and RIbeta regulatory subunits of protein kinase a in vivo by the yeast two hybrid system". J. Mol. Biol. 327 (3): 609–18. doi:10.1016/S0022-2836(03)00093-7. PMID12634056.
Steen RL, Beullens M, Landsverk HB, et al. (2004). "AKAP149 is a novel PP1 specifier required to maintain nuclear envelope integrity in G1 phase". J. Cell Sci. 116 (Pt 11): 2237–46. doi:10.1242/jcs.00432. PMID12697839.
