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 Lettjournal_title
FEBS lettersauthors
Meacci E,Donati C,Cencetti F,Romiti E,Bruni Pdoi
10.1016/s0014-5793(00)02039-1keywords:
subject
Has Abstractpub_date
2000-09-29 00:00:00pages
97-101issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(00)02039-1journal_volume
482pub_type
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