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Activation of mitogen‐activated protein kinase by the bradykinin B 2 receptor is independent of receptor phosphorylation and phosphorylation‐triggered internalization
Author(s) -
Blaukat Andree,
Pizard Anne,
Rajerison Rabary M.,
Alhenc-Gelas François,
Müller-Esterl Werner,
Dikic Ivan
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00613-4
Subject(s) - internalization , phosphorylation , microbiology and biotechnology , chemistry , mitogen activated protein kinase , phosphorylation cascade , protein kinase a , receptor , protein phosphorylation , biochemistry , biology
Recent evidence suggests that serine/threonine phosphorylation and internalization of β 2 ‐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 Gα q ‐coupled bradykinin B 2 receptors. Mutant B 2 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 B 2 receptors. Therefore, G protein‐coupled bradykinin receptors activate the mitogen‐activated protein kinase pathway independently of receptor phosphorylation and internalization.