6533b85ffe1ef96bd12c1d7b
RESEARCH PRODUCT
Activation of mitogen-activated protein kinase by the bradykinin B2receptor is independent of receptor phosphorylation and phosphorylation-triggered internalization
Ivan DikicFrançois Alhenc-gelasWerner Müller-esterlAndree BlaukatRabary M. RajerisonAnne Pizardsubject
Receptor Bradykinin B2Bradykinin B2 receptorBiophysicsMitogen-activated protein kinase kinaseBradykininBiochemistryCell LineMAP2K7Structural BiologyMitogenic signallingGeneticsHumansPhosphorylationBradykinin receptorProtein kinase AMolecular BiologyProtein kinase CG protein-coupled receptorG protein-coupled receptor kinaseMAP kinase kinase kinaseChemistryReceptors BradykininCell BiologyMitogen-activated protein kinaseEnzyme ActivationBiochemistryCalcium-Calmodulin-Dependent Protein KinasesInternalizationSignal Transductiondescription
Recent evidence suggests that serine/threonine phosphorylation and internalization of beta2-adrenergic receptors play critical roles in signalling to the mitogen-activated protein kinase cascade. To investigate whether this represents a general mechanism employed by G protein-coupled receptors, we studied the requirement of these processes in the activation of mitogen-activated protein kinase by G alpha(q)-coupled bradykinin B2 receptors. Mutant B2 receptors impaired in receptor phosphorylation and internalization are fully capable to activate mitogen-activated protein kinase. Bradykinin-induced long-term effects on mitogenic signalling monitored by measuring the transcriptional activity of Elk1 were identical in cells expressing the wild-type or mutant B2 receptors. Therefore, G protein-coupled bradykinin receptors activate the mitogen-activated protein kinase pathway independently of receptor phosphorylation and internalization.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1999-06-17 | FEBS Letters |