Synaptic vesicle mobilization is regulated by distinct synapsin I phosphorylation pathways at different frequencies (Q48337913)

10 February 2018

title

Synaptic vesicle mobilization is regulated by distinct synapsin I phosphorylation pathways at different frequencies (English)

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10 February 2018

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3

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10 February 2018

Paul Greengard

series ordinal

2

object named as

Paul Greengard

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10 February 2018

Ping Chi

1

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10 February 2018

language of work or name

English

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publication date

1 April 2003

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10 February 2018

published in

Neuron

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10 February 2018

volume

38

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10 February 2018

issue

1

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10 February 2018

page(s)

69-78

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10 February 2018

Synapsin I bundles F-actin in a phosphorylation-dependent manner

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Characterization of synapsin I fragments produced by cysteine-specific cleavage: a study of their interactions with F-actin

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Interactions of synapsin I with small synaptic vesicles: distinct sites in synapsin I bind to vesicle phospholipids and vesicle proteins

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Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers

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7 January 2021

Synapsin I, a neuron-specific phosphoprotein interacting with small synaptic vesicles and F-actin

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Interactions of synapsin I with phospholipids: possible role in synaptic vesicle clustering and in the maintenance of bilayer structures

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Dephosphorylated synapsin I anchors synaptic vesicles to actin cytoskeleton: an analysis by videomicroscopy.

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Synapsin dispersion and reclustering during synaptic activity

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Synapsin IIa bundles actin filaments.

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Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I

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[23] Production of phosphorylation state-specific antibodies

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Synapsin I (protein I), a nerve terminal-specific phosphoprotein. I. Its general distribution in synapses of the central and peripheral nervous system demonstrated by immunofluorescence in frozen and plastic sections

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Neuronal phosphoproteins. Mediators of signal transduction

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Synaptic vesicle phosphoproteins and regulation of synaptic function

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Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals

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Two sites of action for synapsin domain E in regulating neurotransmitter release

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Synapsin III, a novel synapsin with an unusual regulation by Ca2+

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Homo- and heterodimerization of synapsins

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A phospho-switch controls the dynamic association of synapsins with synaptic vesicles

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Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation

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Neurotrophins stimulate phosphorylation of synapsin I by MAP kinase and regulate synapsin I-actin interactions

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Opposing changes in phosphorylation of specific sites in synapsin I during Ca2+-dependent glutamate release in isolated nerve terminals.

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A third member of the synapsin gene family

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Molecular evolution of the synapsin gene family

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Synapsins in the vertebrate retina: absence from ribbon synapses and heterogeneous distribution among conventional synapses

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Differential expression of synapsins I and II among rat retinal synapses

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An essential role for protein phosphatases in hippocampal long-term depression

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Inhibitors of myosin light chain kinase block synaptic vesicle pool mobilization during action potential firing

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Synaptic vesicle recycling in synapsin I knock-out mice

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Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system.

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Translocation of synapsin I in response to depolarization of isolated nerve terminals

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Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins

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Regulation of dendritic growth and remodeling by Rho, Rac, and Cdc42.

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Identifiers

DOI

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10 February 2018

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10 February 2018