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Phosphorylated synaphin/complexin found in the brain exhibits enhanced SNARE complex binding.

Abstract：

:The cytosolic protein synaphin/complexin critically regulates fast neurotransmitter release at the synapse by binding to SNARE complex. However, the exact mechanism of its action remains unclear, and very little is known about how it is physiologically regulated. Here we show that synaphins (Syps) 1 and 2 can be phosphorylated in vitro by protein kinase CK2 (CK2). The only phosphorylation site by CK2 was serine-115 (Ser-115) of Syps 1 and 2. Syps 1 and 2 exhibited higher affinities to native and recombinant SNARE complexes when phosphorylated at Ser-115. We found Ser-115-phosphorylated Syp 1 (pS115-Syp 1) in the cytosolic fraction of the rat brain using polyclonal antibody specific to pS115-Syps 1 and 2. These results suggest that the activity of Syp is regulated by CK2 phosphorylation of its Ser-115 in vivo. The phosphorylation may provide a new route for modulating fast neurotransmitter release.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Shata A,Saisu H,Odani S,Abe T

doi

10.1016/j.bbrc.2007.01.064

subject

Has Abstract

pub_date

2007-03-16 00:00:00

pages

808-13

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)00112-X

journal_volume

354

pub_type

杂志文章

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