Title : Plasma membrane subdomain compartmentalization contributes to distinct mechanisms of ceramide action on insulin signaling.

Pub. Date : 2010 Mar

PMID : 19959757






7 Functional Relationships(s)
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1 OBJECTIVE: Ceramide is now recognized as a negative regulator of insulin signaling by impairing protein kinase B (PKB)/Akt activation. Ceramides AKT serine/threonine kinase 1 Homo sapiens
2 OBJECTIVE: Ceramide is now recognized as a negative regulator of insulin signaling by impairing protein kinase B (PKB)/Akt activation. Ceramides AKT serine/threonine kinase 1 Homo sapiens
3 In different cells, two distinct mechanisms have been proposed to mediate ceramide inhibition of PKB/Akt: one involving atypical protein kinase C zeta (PKCzeta) and the other the protein phosphatase-2 (PP2A). Ceramides AKT serine/threonine kinase 1 Homo sapiens
4 In different cells, two distinct mechanisms have been proposed to mediate ceramide inhibition of PKB/Akt: one involving atypical protein kinase C zeta (PKCzeta) and the other the protein phosphatase-2 (PP2A). Ceramides AKT serine/threonine kinase 1 Homo sapiens
5 RESULTS: Although the PKCzeta-mediated negative effect of ceramide on insulin-stimulated PKB/Akt was dominant in adipocytes, a ceramide action through PP2A outside CEMs, prevented by OKA, was also unraveled. Ceramides AKT serine/threonine kinase 1 Homo sapiens
6 CONCLUSIONS: Our results show that ceramide can switch from a PKCzeta-dependent mechanism to a PP2A pathway, acting negatively on PKB/Akt, and hence revealing a critical role of CEMs of the PM in this process. Ceramides AKT serine/threonine kinase 1 Homo sapiens
7 CONCLUSIONS: Our results show that ceramide can switch from a PKCzeta-dependent mechanism to a PP2A pathway, acting negatively on PKB/Akt, and hence revealing a critical role of CEMs of the PM in this process. Ceramides AKT serine/threonine kinase 1 Homo sapiens