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CB1 cannabinoid receptor‐mediated tyrosine phosphorylation of focal adhesion kinase‐related non‐kinase
Author(s) -
Zhou Dan,
Song Z.H
Publication year - 2002
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(02)03091-0
Subject(s) - chemistry , receptor tyrosine kinase , tropomyosin receptor kinase c , microbiology and biotechnology , focal adhesion , phosphorylation , cannabinoid receptor , ror1 , tyrosine kinase , ptk2 , platelet derived growth factor receptor , mitogen activated protein kinase kinase , biochemistry , signal transduction , receptor , biology , protein kinase a , growth factor , agonist
The effect of cannabinoid on the tyrosine phosphorylation of focal adhesion kinase (FAK) and focal adhesion kinase‐related non‐kinase (FRNK) was investigated in differentiated mouse neuroblastoma N1E‐115 cells. HU‐210, a potent cannabinoid agonist, elicited a time‐dependent enhancement of tyrosine phosphorylation of FRNK, but not FAK. Pretreatment of cells with antisense oligodeoxynucleotide targeting CB1 cannabinoid receptor abolished HU‐210‐induced FRNK tyrosine phosphorylation. In addition, pretreatment of cells with 8‐Br‐cAMP also blocked HU‐210‐induced FRNK tyrosine phosphorylation. These data demonstrated that HU‐210 induces FRNK tyrosine phosphorylation by activating G i ‐coupled CB1 cannabinoid receptor in N1E‐115 cells. This newly discovered, cannabinoid‐induced FRNK tyrosine phosphorylation might be a novel mechanism for cannabinoid‐induced functional changes.