Permissive role of protein kinase C alpha but not protein kinase C delta in sphingosine 1-phosphate-induced Rho A activation in C2C12 myoblasts.

Abstract:

: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 Rho A in a pertussis toxin-insensitive manner. The bioactive lipid preferentially relocalized the GTPase to Golgi-enriched membrane. Translocation of Rho A was abolished by inhibition or down-regulation of protein kinase C (PKC). Notably, treatment with Gö6976, an inhibitor of conventional PKCs, which selectively blocked PKC alpha in these cells, prevented SPP-induced Rho A translocation. Conversely rottlerin, a selective inhibitor of PKC delta, was without effect, demonstrating that SPP signaling to Rho A involves PKC alpha but not PKC delta activation. This novel functional relationship between the two proteins may have a role in SPP-mediated regulation of downstream effectors.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Meacci E,Donati C,Cencetti F,Romiti E,Bruni P

doi

10.1016/s0014-5793(00)02039-1

keywords:

subject

Has Abstract

pub_date

2000-09-29 00:00:00

pages

97-101

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(00)02039-1

journal_volume

482

pub_type

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