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Phosphorylation of cysteine string protein in the brain: developmental, regional and synaptic specificity
Author(s) -
Evans Gareth J. O.,
Morgan Alan
Publication year - 2005
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.2005.04118.x
Subject(s) - neuroscience , phosphorylation , cysteine , chemistry , biology , microbiology and biotechnology , biochemistry , enzyme
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.