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PMID: 9163333 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Regulation by bivalent cations of phospholipid binding to the C2A domain of synaptotagmin III.

The Biochemical journal ·Vol. 323 ( Pt 2) ·1997-04-15 ·Pages 421-5

Fukuda M, Kojima T, Mikoshiba K

Abstract

Synaptotagmins are Ca2+-and phospholipid-binding proteins of synaptic vesicles that might function as Ca2+ receptors for neurotransmitter release via their first C2 (C2A) domain. Here we describe the effect of Mg2+ on phospholipid binding to the C2A domains of multiple synaptotagmins (II-VI), and demonstrate that only synaptotagmin III can bind negatively charged phospholipids [phosphatidylserine (PS) and phosphatidylinositol] in a Mg2+-dependent manner. The Mg2+-dependent interaction with PS was found to have an EC50 of approx. 30 microM Mg2+, which is comparable to that of Sr2+ and Ba2+ (EC50 values of approx. 10 microM). This binding property of the C2A domain is specific to synaptotagmin III, because none of the C2A domains of other proteins, such as rabphilin 3A, Doc2alpha, Doc2beta or Gap1(m), showed phospholipid binding activity in the presence of 1 mM Mg2+. Our results suggest that synaptotagmin III is involved in presynaptic functions different from those of synaptotagmins I and II.

MeSH Terms
Amino Acid Sequence Animals Barium/pharmacology Binding Sites Calcium-Binding Proteins Carrier Proteins/metabolism Liposomes/metabolism Magnesium/pharmacology Membrane Glycoproteins/metabolism Membrane Proteins/metabolism Mice Molecular Sequence Data Nerve Tissue Proteins/metabolism Phospholipids/metabolism Sequence Alignment Strontium/pharmacology Synaptotagmin II Synaptotagmins
Chemicals
Calcium-Binding Proteins Carrier Proteins Liposomes Membrane Glycoproteins Membrane Proteins Nerve Tissue Proteins Phospholipids Synaptotagmin II Syt2 protein, mouse Syt3 protein, mouse Synaptotagmins Barium Magnesium Strontium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fukuda M
Molecular Neurobiology Laboratory, Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1-1 Koyadai, Tsukuba, Ibaraki 305, Japan.
Kojima T
Mikoshiba K
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1997-04-15
Pages
421-5
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1218336
Subset
IM
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