Activation of mitogen-activated protein kinase by the bradykinin B2 receptor is independent of receptor phosphorylation and phosphorylation-triggered internalization

FEBS Lett. 1999 May 28;451(3):337-41. doi: 10.1016/s0014-5793(99)00613-4.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bradykinin / pharmacology*
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Cell Line
  • Enzyme Activation
  • Humans
  • Phosphorylation
  • Receptor, Bradykinin B2
  • Receptors, Bradykinin / agonists
  • Receptors, Bradykinin / metabolism*
  • Signal Transduction* / drug effects


  • Receptor, Bradykinin B2
  • Receptors, Bradykinin
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Bradykinin