Phosphorylation of synapsin I and MARCKS in nerve terminals is mediated by Ca2+ entry via an Aga-GI sensitive Ca2+ channel which is coupled to glutamate exocytosis

E T Coffey; T S Sihra; D G Nicholls; J M Pocock

doi:10.1016/0014-5793(94)01061-7

Phosphorylation of synapsin I and MARCKS in nerve terminals is mediated by Ca2+ entry via an Aga-GI sensitive Ca2+ channel which is coupled to glutamate exocytosis

E T Coffey, T S Sihra, D G Nicholls, J M Pocock

Turku Bioscience Centre

Research output: Contribution to journal › Article › Scientific › peer-review

31 Citations (Scopus)

Abstract

Ca2+ entry is a prerequisite for both exocytosis and the phosphorylation of synapsin I and MARCKS proteins in mammalian cerebrocortical synaptosomes. The novel spider toxin Aga-GI completely blocks KCl-evoked glutamate exocytosis but only partially inhibits KCl-evoked cytoplasmic Ca2+ elevations, thus revealing at least two pathways for KCl-induced Ca2+ entry. Aga-GI completely attenuates KCl-induced phosphorylation of synapsin I and MARCKS proteins. We therefore conclude that both exocytosis and the phosphorylation of synapsin I and MARCKS proteins are specifically coupled to Ca2+ entry via a subset of voltage dependent Ca2+ channels at the nerve terminal which are sensitive to Aga-GI.

Original language	English
Pages (from-to)	264-8
Number of pages	5
Journal	FEBS Letters
Volume	353
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(94)01061-7
Publication status	Published - 24 Oct 1994
MoE publication type	A1 Journal article-refereed

Keywords

Animals
Calcium/metabolism
Calcium Channels/drug effects
Cerebral Cortex/metabolism
Exocytosis/drug effects
Glutamic Acid/metabolism
Intracellular Signaling Peptides and Proteins
Male
Membrane Proteins
Myristoylated Alanine-Rich C Kinase Substrate
Phosphorylation
Potassium Chloride/pharmacology
Protein Kinase C/metabolism
Proteins/metabolism
Rats
Rats, Wistar
Spider Venoms/pharmacology
Synapsins/metabolism
Synaptosomes/metabolism

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10.1016/0014-5793(94)01061-7

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title = "Phosphorylation of synapsin I and MARCKS in nerve terminals is mediated by Ca2+ entry via an Aga-GI sensitive Ca2+ channel which is coupled to glutamate exocytosis",

abstract = "Ca2+ entry is a prerequisite for both exocytosis and the phosphorylation of synapsin I and MARCKS proteins in mammalian cerebrocortical synaptosomes. The novel spider toxin Aga-GI completely blocks KCl-evoked glutamate exocytosis but only partially inhibits KCl-evoked cytoplasmic Ca2+ elevations, thus revealing at least two pathways for KCl-induced Ca2+ entry. Aga-GI completely attenuates KCl-induced phosphorylation of synapsin I and MARCKS proteins. We therefore conclude that both exocytosis and the phosphorylation of synapsin I and MARCKS proteins are specifically coupled to Ca2+ entry via a subset of voltage dependent Ca2+ channels at the nerve terminal which are sensitive to Aga-GI.",

keywords = "Animals, Calcium/metabolism, Calcium Channels/drug effects, Cerebral Cortex/metabolism, Exocytosis/drug effects, Glutamic Acid/metabolism, Intracellular Signaling Peptides and Proteins, Male, Membrane Proteins, Myristoylated Alanine-Rich C Kinase Substrate, Phosphorylation, Potassium Chloride/pharmacology, Protein Kinase C/metabolism, Proteins/metabolism, Rats, Rats, Wistar, Spider Venoms/pharmacology, Synapsins/metabolism, Synaptosomes/metabolism",

author = "Coffey, {E T} and Sihra, {T S} and Nicholls, {D G} and Pocock, {J M}",

year = "1994",

month = oct,

day = "24",

doi = "10.1016/0014-5793(94)01061-7",

language = "English",

volume = "353",

pages = "264--8",

journal = "FEBS Letters",

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number = "3",

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T1 - Phosphorylation of synapsin I and MARCKS in nerve terminals is mediated by Ca2+ entry via an Aga-GI sensitive Ca2+ channel which is coupled to glutamate exocytosis

AU - Coffey, E T

AU - Sihra, T S

AU - Nicholls, D G

AU - Pocock, J M

PY - 1994/10/24

Y1 - 1994/10/24

N2 - Ca2+ entry is a prerequisite for both exocytosis and the phosphorylation of synapsin I and MARCKS proteins in mammalian cerebrocortical synaptosomes. The novel spider toxin Aga-GI completely blocks KCl-evoked glutamate exocytosis but only partially inhibits KCl-evoked cytoplasmic Ca2+ elevations, thus revealing at least two pathways for KCl-induced Ca2+ entry. Aga-GI completely attenuates KCl-induced phosphorylation of synapsin I and MARCKS proteins. We therefore conclude that both exocytosis and the phosphorylation of synapsin I and MARCKS proteins are specifically coupled to Ca2+ entry via a subset of voltage dependent Ca2+ channels at the nerve terminal which are sensitive to Aga-GI.

AB - Ca2+ entry is a prerequisite for both exocytosis and the phosphorylation of synapsin I and MARCKS proteins in mammalian cerebrocortical synaptosomes. The novel spider toxin Aga-GI completely blocks KCl-evoked glutamate exocytosis but only partially inhibits KCl-evoked cytoplasmic Ca2+ elevations, thus revealing at least two pathways for KCl-induced Ca2+ entry. Aga-GI completely attenuates KCl-induced phosphorylation of synapsin I and MARCKS proteins. We therefore conclude that both exocytosis and the phosphorylation of synapsin I and MARCKS proteins are specifically coupled to Ca2+ entry via a subset of voltage dependent Ca2+ channels at the nerve terminal which are sensitive to Aga-GI.

KW - Animals

KW - Calcium/metabolism

KW - Calcium Channels/drug effects

KW - Cerebral Cortex/metabolism

KW - Exocytosis/drug effects

KW - Glutamic Acid/metabolism

KW - Intracellular Signaling Peptides and Proteins

KW - Male

KW - Membrane Proteins

KW - Myristoylated Alanine-Rich C Kinase Substrate

KW - Phosphorylation

KW - Potassium Chloride/pharmacology

KW - Protein Kinase C/metabolism

KW - Proteins/metabolism

KW - Rats

KW - Rats, Wistar

KW - Spider Venoms/pharmacology

KW - Synapsins/metabolism

KW - Synaptosomes/metabolism

U2 - 10.1016/0014-5793(94)01061-7

DO - 10.1016/0014-5793(94)01061-7

M3 - Article

C2 - 7957871

SN - 0014-5793

VL - 353

SP - 264

EP - 268

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Phosphorylation of synapsin I and MARCKS in nerve terminals is mediated by Ca2+ entry via an Aga-GI sensitive Ca2+ channel which is coupled to glutamate exocytosis

Abstract

Keywords

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