Sphingosine and ceramide signalling in apoptosis
Open Access
- 1 August 2006
- journal article
- review article
- Published by Wiley in IUBMB Life
- Vol. 58 (8) , 462-466
- https://doi.org/10.1080/15216540600871118
Abstract
The sphingomyelin pathway is activated in response to many apoptotic stimuli leading to the accumulation of breakdown products ceramide and sphingosine. Ceramide has received much attention as an apoptotic second messenger whereas sphingosine has largely been overlooked as a mediator of apoptosis. Recent studies however provide strong clues to a second messenger role for sphingosine and identification of effectors reveal a possible mechanism involved in sphingosine‐mediated cell death. This mini‐review overviews the current knowledge of the role of ceramide and sphingosine in apoptosis and discusses their biological effects. The review attempts to reconcile the apoptotic effects of these lipids with the downstream effectors that have been identified. iubmb Life, 58: 462 ‐ 466, 2006Keywords
This publication has 10 references indexed in Scilit:
- Sphingosine Activates Protein Kinase A Type II by a Novel cAMP-independent MechanismJournal of Biological Chemistry, 2005
- Caspase-dependent and -independent Activation of Acid Sphingomyelinase SignalingJournal of Biological Chemistry, 2005
- Mitochondrial Ceramide and the Induction of ApoptosisJournal of Bioenergetics and Biomembranes, 2005
- Sphingosine-dependent Protein Kinase-1, Directed to 14-3-3, Is Identified as the Kinase Domain of Protein Kinase CδJournal of Biological Chemistry, 2003
- The Dimeric Versus Monomeric Status of 14-3-3ζ Is Controlled by Phosphorylation of Ser58 at the Dimer InterfaceJournal of Biological Chemistry, 2003
- Sphingolipids in mammalian cell signallingCellular and Molecular Life Sciences, 2001
- Sphingosine Is a Novel Activator of 3-Phosphoinositide-dependent Kinase 1Journal of Biological Chemistry, 2000
- Sphingolipid signalling domains Floating on rafts or buried in caves?Cellular Signalling, 2000
- A Novel Sphingosine-dependent Protein Kinase (SDK1) Specifically Phosphorylates Certain Isoforms of 14-3-3 ProteinJournal of Biological Chemistry, 1998
- A GTPase-independent Mechanism of p21-activated Kinase ActivationJournal of Biological Chemistry, 1998