Permissive role of protein kinase Cα but not protein kinase Cδ in sphingosine 1‐phosphate‐induced RhoA activation in C2C12 myoblasts

FEBS Letters

Meacci, Elisabetta¹  Cencetti, Francesca¹  Bruni, Paola¹  Romiti, Elena¹  Donati, Chiara¹ 

[1] Dipartimento di Scienze Biochimiche, Università di Firenze, Viale G.B. Morgagni 50, 50134 Florence, Italy

关键词: Sphingosine 1-phosphate;    RhoA;    C2C12 myoblast;    Protein kinase Cα;    SPP;    sphingosine 1-phosphate;    Edg;    endothelial differentiation gene;    PKC;    protein kinase C;    TTBS;    Tris-buffered saline containing 0.1% Tween-20;    CELM;    caveolin-enriched light membrane;    PTx;    pertussis toxin;   

DOI  :  10.1016/S0014-5793(00)02039-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rho GTPases participate in various important signaling pathways and have been implicated in myogenic differentiation. Here the first evidence is provided that in C2C12 myoblasts sphingosine 1-phosphate (SPP) rapidly and transiently induced membrane association of RhoA in a pertussis toxin-insensitive manner. The bioactive lipid preferentially relocalized the GTPase to Golgi-enriched membrane. Translocation of RhoA was abolished by inhibition or down-regulation of protein kinase C (PKC). Notably, treatment with Gö6976, an inhibitor of conventional PKCs, which selectively blocked PKCα in these cells, prevented SPP-induced RhoA translocation. Conversely rottlerin, a selective inhibitor of PKCδ, was without effect, demonstrating that SPP signaling to RhoA involves PKCα but not PKCδ activation. This novel functional relationship between the two proteins may have a role in SPP-mediated regulation of downstream effectors.

【 授权许可】

Unknown