TY - JOUR
T1 - Phosphorylation of cysteine string protein in the brain
T2 - developmental, regional and synaptic specificity
AU - Evans, G J O
AU - Morgan, A
PY - 2005/5
Y1 - 2005/5
N2 - Protein phosphorylation modulates regulated exocytosis in most cells, including neurons. Cysteine string protein (CSP) has been implicated in this process because its phosphorylation on Ser(10) alters its interactions with syntaxin and synaptotagmin, and because the effect of CSP overexpression on exocytosis kinetics in chromaffin cells requires phosphorylatable Ser(10). To characterize CSP phosphorylation in the brain, we raised phosphospecific antibodies to Ser(10). Western blotting revealed that the proportion of phosphorylated CSP (P-CSP) varies between distinct brain regions and also exhibits developmental regulation, with P-CSP highest early in development. Immunohistochemical analysis of the cerebellar cortex revealed a novel pool of P-CSP that did not colocalize with synaptic vesicle markers during early development. Strikingly, in the adult cerebellar granular layer P-CSP was highly enriched in a subset of glutamatergic synapses but undetectable in neighbouring GABA-ergic synapses. In view of the functional consequences of CSP phosphorylation, such differences could contribute to the synapse-specific regulation of neurotransmitter release.
AB - Protein phosphorylation modulates regulated exocytosis in most cells, including neurons. Cysteine string protein (CSP) has been implicated in this process because its phosphorylation on Ser(10) alters its interactions with syntaxin and synaptotagmin, and because the effect of CSP overexpression on exocytosis kinetics in chromaffin cells requires phosphorylatable Ser(10). To characterize CSP phosphorylation in the brain, we raised phosphospecific antibodies to Ser(10). Western blotting revealed that the proportion of phosphorylated CSP (P-CSP) varies between distinct brain regions and also exhibits developmental regulation, with P-CSP highest early in development. Immunohistochemical analysis of the cerebellar cortex revealed a novel pool of P-CSP that did not colocalize with synaptic vesicle markers during early development. Strikingly, in the adult cerebellar granular layer P-CSP was highly enriched in a subset of glutamatergic synapses but undetectable in neighbouring GABA-ergic synapses. In view of the functional consequences of CSP phosphorylation, such differences could contribute to the synapse-specific regulation of neurotransmitter release.
U2 - 10.1111/j.1460-9568.2005.04118.x
DO - 10.1111/j.1460-9568.2005.04118.x
M3 - Article
SN - 0953-816X
VL - 21
SP - 2671
EP - 2680
JO - The European Journal of Neuroscience
JF - The European Journal of Neuroscience
IS - 10
ER -