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Electrostatic regulation of the cis - and trans -membrane interactions of synaptotagmin-1
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Abstract
Synaptotagmin-1 is a vesicular protein and Ca
2+
sensor for Ca
2+
-dependent exocytosis. Ca
2+
induces synaptotagmin-1 binding to its own vesicle membrane, called the
cis-
interaction, thus preventing the
trans
-interaction of synaptotagmin-1 to the plasma membrane. However, the electrostatic regulation of the
cis
- and
trans
-membrane interaction of synaptotagmin-1 was poorly understood in different Ca
2+
-buffering conditions. Here we provide an assay to monitor the
cis
- and
trans
-membrane interactions of synaptotagmin-1 by using native purified vesicles and the plasma membrane-mimicking liposomes (PM-liposomes). Both ATP and EGTA similarly reverse the
cis
-membrane interaction of synaptotagmin-1 in free [Ca
2+
] of 10 to 100 μM. High PIP
2
concentrations in the PM-liposomes reduce the Hill coefficient of vesicle fusion and synaptotagmin-1 membrane binding; this observation suggests that local PIP
2
concentrations control the Ca
2+
-cooperativity of synaptotagmin-1. Our data provide evidence that Ca
2+
chelators, including EGTA and polyphosphate anions such as ATP, ADP, and AMP, electrostatically reverse the
cis
-interaction of synaptotagmin-1.
Title: Electrostatic regulation of the
cis
- and
trans
-membrane interactions of synaptotagmin-1
Description:
Abstract
Synaptotagmin-1 is a vesicular protein and Ca
2+
sensor for Ca
2+
-dependent exocytosis.
Ca
2+
induces synaptotagmin-1 binding to its own vesicle membrane, called the
cis-
interaction, thus preventing the
trans
-interaction of synaptotagmin-1 to the plasma membrane.
However, the electrostatic regulation of the
cis
- and
trans
-membrane interaction of synaptotagmin-1 was poorly understood in different Ca
2+
-buffering conditions.
Here we provide an assay to monitor the
cis
- and
trans
-membrane interactions of synaptotagmin-1 by using native purified vesicles and the plasma membrane-mimicking liposomes (PM-liposomes).
Both ATP and EGTA similarly reverse the
cis
-membrane interaction of synaptotagmin-1 in free [Ca
2+
] of 10 to 100 μM.
High PIP
2
concentrations in the PM-liposomes reduce the Hill coefficient of vesicle fusion and synaptotagmin-1 membrane binding; this observation suggests that local PIP
2
concentrations control the Ca
2+
-cooperativity of synaptotagmin-1.
Our data provide evidence that Ca
2+
chelators, including EGTA and polyphosphate anions such as ATP, ADP, and AMP, electrostatically reverse the
cis
-interaction of synaptotagmin-1.
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