RGD Reference Report - Protein kinase C-mediated phosphorylation of a single serine residue on the rat glial glutamine transporter SN1 governs its membrane trafficking. - Rat Genome Database

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Protein kinase C-mediated phosphorylation of a single serine residue on the rat glial glutamine transporter SN1 governs its membrane trafficking.

Authors: Nissen-Meyer, Lise Sofie H  Popescu, Mark C  Hamdani, El Hassan  Chaudhry, Farrukh A 
Citation: Nissen-Meyer LS, etal., J Neurosci. 2011 Apr 27;31(17):6565-75. doi: 10.1523/JNEUROSCI.3694-10.2011.
RGD ID: 152995537
Pubmed: PMID:21525297   (View Abstract at PubMed)
PMCID: PMC6622677   (View Article at PubMed Central)
DOI: DOI:10.1523/JNEUROSCI.3694-10.2011   (Journal Full-text)

Molecular mechanisms involved in the replenishment of the fast neurotransmitters glutamate and GABA are poorly understood. Glutamine sustains their generation. However, glutamine formation from the recycled transmitters is confined to glial processes and requires facilitators for its translocation across the glial and neuronal membranes. Indeed, glial processes are enriched with the system N transporter SN1 (Slc38a3), which, by bidirectional transport, maintains steady extracellular glutamine levels and thereby furnishes neurons with the primary precursor for fast neurotransmitters. We now demonstrate that SN1 is phosphorylated by protein kinase Cα (PKCα) and PKCγ. Electrophysiological characterization shows that phosphorylation reduces V(max) dramatically, whereas no significant effects are seen on the K(m). Phosphorylation occurs specifically at a single serine residue (S52) in the N-terminal rat (Rattus norvegicus) SN1 and results in sequestration of the protein into intracellular reservoirs. Prolonged activation of PKC results in partial degradation of SN1. These results provide the first demonstration of phosphorylation of SN1 and regulation of its activity at the plasma membrane. Interestingly, membrane trafficking of SN1 resembles that of the glutamate transporter GLT and the glutamate-aspartate transporter GLAST: it involves the same PKC isoforms and occurs in the same glial processes. This suggests that the glutamate/GABA-glutamine cycle may be modified at two key points by similar signaling events and unmasks a prominent role for PKC-dependent phosphorylation. Our data suggest that extracellular glutamine levels may be fine-tuned by dynamic regulation of glial SN1 activity, which may impact on transmitter generation, contribute to defining quantal size, and have profound effects on synaptic plasticity.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Slc38a3RatL-asparagine import across plasma membrane involved_inIDA PMID:21525297UniProt 
Slc38a3RatL-glutamine import across plasma membrane involved_inIDA PMID:21525297UniProt 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Slc38a3Ratplasma membrane located_inIDA PMID:21525297UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Slc38a3RatL-asparagine, sodium:proton antiporter activity enablesIDA PMID:21525297UniProt 
Slc38a3RatL-glutamine, sodium:proton antiporter activity enablesIDA PMID:21525297UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Slc38a3  (solute carrier family 38, member 3)


Additional Information