Stathminisaubiquitous,cytosolic19-kDaprotein,whichisphosphorylatedonuptofoursitesinresponsetomanyregulatorysignalswithincells.ItsmolecularcharacterizationindicatesafunctionalorganizationincludinganN-terminalregulatorydomainthatbearsthephosphorylationsites,linkedtoaputativealpha-helicalbindingdomainpredictedtoparticipateincoiled-coil,protein-proteininteractions.InaddtiontotheproteinkinasesthatphospjhorylateStathminsuchasCaMK,MAPK,p34cdc2,PKA,afewotherproteinshavebeensuggestedtointeractwithstathmininvivo.OneofthemwasidentifiedasBiP,amemberofthehsp70heat-shockproteinfamily.Anotherisapreviouslyunidentified,putativeserine/threoninekinase,KIS,whichmightberegulatedbystathminor,morelikely,bepartofthekinasescontrollingitsphosphorylationstate.Finally,twoproteins,CC1andCC2,predictedtoformalpha-helicesparticipatingincoiled-coilinteractingstructures.Ithasbeenalsosuggestthattheactionofantimicrotubuledrugscanbeaffectedbystathmininatleasttwoways:(a)altereddrugbinding;and(b)growtharrestattheG2toMboundary.Mutantp53breastcancersexhibitinghighlevelsofstathminmayberesistanttoantimicrotubuleagents.

Contributor:KosiGramatikoff,PhD

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