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PMID: 7654227 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Synaphin: a protein associated with the docking/fusion complex in presynaptic terminals.

Biochemical and biophysical research communications ·Vol. 213 ·No. 3 ·1995-08-24 ·Pages 1107-14

Ishizuka T, Saisu H, Odani S, Abe T

Abstract

We previously identified a 19 kDa protein associated with the docking/fusion complex involved in neurotransmitter release. A cDNA for this protein was cloned from a bovine brain cDNA library using an oligonucleotide probe based on its partial amino acid sequence. The protein (named synaphin) encoded by the cDNA is a very hydrophilic protein rich in glutamic acid and lysine residues. It lacks any putative transmembrane segments or strongly hydrophobic domains. Immunoblots with antibodies against synaphin detected the protein only in the nervous system among the tissues examined. In brain, it exists mainly in the soluble fraction and is scarce in synaptic vesicles.

MeSH Terms
Adaptor Proteins, Vesicular Transport Amino Acid Sequence Animals Base Sequence Cattle Cloning, Molecular DNA, Complementary Molecular Sequence Data Nerve Tissue Proteins/genetics,metabolism Presynaptic Terminals/metabolism Protein Binding Subcellular Fractions/metabolism
Chemicals
Adaptor Proteins, Vesicular Transport DNA, Complementary Nerve Tissue Proteins complexin II
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ishizuka T
Department of Cellular Neurobiology, Faculty of Science, Niigata University, Japan.
Saisu H
Odani S
Abe T
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1995-08-24
Pages
1107-14
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Databases
GENBANK
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