Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neurons

Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neurons

Protein domains play a fundamental role in the spatial and temporal organization of intracellular signaling systems. While protein phosphorylation has long been known to modify the interactions that underlie this organization, the dynamic cycling of lipids should now be included amongst the posttranslational processes determining specificity in signal transduction. The characteristics of this process are reminiscent of the properties of protein and lipid phosphorylation in determining compartmentalization through SH2 or PH domains. Recent studies have confirmed the functional importance of protein S-palmitoylation in the compartmentalization of signaling molecules that support normal physiological function in cell division and apoptosis, and synaptic transmission and neurite outgrowth. In neurons, S-palmitoylation and targeting of proteins to rafts are regulated differentially in development by a number of processes, including some related to synaptogenesis and synaptic plasticity. Alterations in the S-palmitoylation state of proteins substantially affect their cellular function, raising the possibility of new therapeutic targets in cancer and nervous system injury and disease.

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Main Author: PATTERSON,SEAN I
Format: Digital revista
Language:English
Published: Sociedad de Biología de Chile 2002
Online Access:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200005
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spelling oai:scielo:S0716-976020020002000052002-12-26Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neuronsPATTERSON,SEAN I S-palmitoylation synapse growth cone regeneration phosphorylation Protein domains play a fundamental role in the spatial and temporal organization of intracellular signaling systems. While protein phosphorylation has long been known to modify the interactions that underlie this organization, the dynamic cycling of lipids should now be included amongst the posttranslational processes determining specificity in signal transduction. The characteristics of this process are reminiscent of the properties of protein and lipid phosphorylation in determining compartmentalization through SH2 or PH domains. Recent studies have confirmed the functional importance of protein S-palmitoylation in the compartmentalization of signaling molecules that support normal physiological function in cell division and apoptosis, and synaptic transmission and neurite outgrowth. In neurons, S-palmitoylation and targeting of proteins to rafts are regulated differentially in development by a number of processes, including some related to synaptogenesis and synaptic plasticity. Alterations in the S-palmitoylation state of proteins substantially affect their cellular function, raising the possibility of new therapeutic targets in cancer and nervous system injury and disease.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.35 n.2 20022002-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200005en10.4067/S0716-97602002000200005
institution SCIELO
collection OJS
country Chile
countrycode CL
component Revista
access En linea
databasecode rev-scielo-cl
tag revista
region America del Sur
libraryname SciELO
language English
format Digital
author PATTERSON,SEAN I
spellingShingle PATTERSON,SEAN I
Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neurons
author_facet PATTERSON,SEAN I
author_sort PATTERSON,SEAN I
title Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neurons
title_short Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neurons
title_full Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neurons
title_fullStr Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neurons
title_full_unstemmed Posttranslational protein S-palmitoylation and the compartmentalization of signaling molecules in neurons
title_sort posttranslational protein s-palmitoylation and the compartmentalization of signaling molecules in neurons
description Protein domains play a fundamental role in the spatial and temporal organization of intracellular signaling systems. While protein phosphorylation has long been known to modify the interactions that underlie this organization, the dynamic cycling of lipids should now be included amongst the posttranslational processes determining specificity in signal transduction. The characteristics of this process are reminiscent of the properties of protein and lipid phosphorylation in determining compartmentalization through SH2 or PH domains. Recent studies have confirmed the functional importance of protein S-palmitoylation in the compartmentalization of signaling molecules that support normal physiological function in cell division and apoptosis, and synaptic transmission and neurite outgrowth. In neurons, S-palmitoylation and targeting of proteins to rafts are regulated differentially in development by a number of processes, including some related to synaptogenesis and synaptic plasticity. Alterations in the S-palmitoylation state of proteins substantially affect their cellular function, raising the possibility of new therapeutic targets in cancer and nervous system injury and disease.
publisher Sociedad de Biología de Chile
publishDate 2002
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200005
work_keys_str_mv AT pattersonseani posttranslationalproteinspalmitoylationandthecompartmentalizationofsignalingmoleculesinneurons
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