TheA-kinaseanchorprotein13(AKAP13,alsoknownasAKAP-LBC)isoneofagroupofstructurallydiverseproteins,whichhavethecommonfunctionofbindingtotheregulatorysubunitofproteinkinaseA(PKA)andconfiningtheholoenzymetodiscretelocationswithinthecell.AKAP13isasplicevariantoftheoncogeneLbc.AlternativesplicingoftheAKAP13generesultsinatleast3transcriptvariantsencodingdifferentisoformscontainingaDbloncogenehomology(DH)domainandapleckstrinhomology(PH)domain.TheDHdomainisassociatedwithguaninenucleotideexchangeactivationfortheRho/RacfamilyofsmallGTPbindingproteins,resultingintheconversionoftheinactiveGTPasetotheactiveformcapableoftransducingsignals.ThePHdomainhasmultiplefunctions.ThesesplicevariantscontainafragmentthatwasoriginallyidentifiedasHt31(SeeCarretal1991)whichactsasascaffoldingproteintoregulatetheRhosignalingpathwayandasproteinkinaseA-anchoringproteincreatingacoordinationofthesetwosignallingpathways.Divianietal.foundthatinHEK293cellsLPAinducedstimulationpreferentiallyactivatesAKAP13viaG-alpha12.AsyettargetsfortheanchoredPKAhavenotbeenidentified.AKAP13andRhodonotappeartobephosphorylatedbyPKA.DivianietalalsofoundthattheLbconcogeneandprotooncogenesplicevariantshowhigheractivationandstressfiberlocalization.ThisappearstobearesultofthepresenceofNterminalinhibitorysequences.AsimilarmodelofregulationhasbeenproposedforDblandVav.

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REFERENCES:CarrDW,Stofko-HahnRE,FraserID,BishopSM,AcottTS,BrennanRG,ScottJD.Interactionoftheregulatorysubunit(RII)ofcAMP-dependentproteinkinasewithRII-anchoringproteinsoccursthroughanamphipathichelixbindingmotif.JBiolChem1991Aug5;266(22):14188-92DivianiD,SoderlingJ,ScottJDAKAP-LbcanchorsproteinkinaseAandnucleatesGalpha12-selectiveRho-mediatedstressfiberformation.JBiolChem.2001Nov23;276(47):44247-57

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