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Receptor‐activated phospholipase D is present in caveolin‐3‐enriched light membranes of C2C12 myotubes
Author(s) -
Meacci Elisabetta,
Donati Chiara,
Cencetti Francesca,
Romiti Elena,
Farnararo Marta,
Bruni Paola
Publication year - 2000
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(00)01486-1
Subject(s) - protein kinase c , phospholipase d , myogenesis , rhoa , phospholipase c , chemistry , c2c12 , microbiology and biotechnology , diacylglycerol kinase , bradykinin , biochemistry , receptor , signal transduction , myocyte , biology
Caveolin‐3 (cav‐3) is a key structural component of caveolar membrane in skeletal muscle. Cav‐3‐enriched light membrane (CELM) fractions obtained from C2C12 myotubes contain phospholipase D1 (PLD1) and its major regulators, RhoA and protein kinase Cα (PKCα). All these proteins were found bound to cav‐3. An in vivo assay of PLD activity, which allows to localize the reaction product in CELMs, indicated that the enzyme associated to this membrane microdomain was active. Moreover, bradykinin (BK), thrombin and phorbol 12‐myristate 13‐acetate induced rapid stimulation of PLD activity in CELMs. The cav‐3‐PLD1 complex was not affected by BK treatment, whereas the agonist induced a marked increase of RhoA association with cav‐3. Furthermore, BK‐induced PLD activation in CELMs was dependent, at least in part, on PKCα.