PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. (Q55038004)

16 June 2018

title

PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. (English)

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16 June 2018

author name string

Jihong Bai

series ordinal

1

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16 June 2018

Ward C Tucker

series ordinal

2

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16 June 2018

Edwin R Chapman

series ordinal

3

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16 June 2018

publication date

29 December 2003

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16 June 2018

Nature Structural & Molecular Biology

published in

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16 June 2018

volume

11

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16 June 2018

issue

1

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page(s)

36-44

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16 June 2018

How does calcium trigger neurotransmitter release?

cites work

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Silent synapses speak up.

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Multivesicular release from excitatory synapses of cultured hippocampal neurons

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Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation

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A developmental switch in neurotransmitter flux enhances synaptic efficacy by affecting AMPA receptor activation

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Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C

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Genomic analysis of synaptotagmin genes

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Synaptotagmin: a calcium sensor on the synaptic vesicle surface

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Synaptotagmin: a Ca(2+) sensor that triggers exocytosis?

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Synaptotagmin I functions as a calcium regulator of release probability

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The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo.

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Synaptotagmins I and IV promote transmitter release independently of Ca(2+) binding in the C(2)A domain

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Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release.

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Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles

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Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin

21 January 2018

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A Pleckstrin Homology Domain Specific for Phosphatidylinositol 4,5-Bisphosphate (PtdIns-4,5-P2) and Fused to Green Fluorescent Protein Identifies Plasma Membrane PtdIns-4,5-P2as Being Important in Exocytosis

21 January 2018

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Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity.

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Evidence that the inositol phospholipids are necessary for exocytosis. Loss of inositol phospholipids and inhibition of secretion in permeabilized cells caused by a bacterial phospholipase C and removal of ATP.

21 January 2018

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Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion

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ATP-dependent inositide phosphorylation required for Ca2+-activated secretion

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PIP(2) and proteins: interactions, organization, and information flow

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C2A activates a cryptic Ca(2+)-triggered membrane penetration activity within the C2B domain of synaptotagmin I.

21 January 2018

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Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine

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Visualization of synaptotagmin I oligomers assembled onto lipid monolayers.

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Functional diversity of C2 domains of synaptotagmin family. Mutational analysis of inositol high polyphosphate binding domain.

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The C2B domain of synaptotagmin is a Ca(2+)-sensing module essential for exocytosis

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Identification of synaptotagmin effectors via acute inhibition of secretion from cracked PC12 cells

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Role of the C2B domain of synaptotagmin in vesicular release and recycling as determined by specific antibody injection into the squid giant synapse preterminal.

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Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis

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Rabphilin-3A: a multifunctional regulator of synaptic vesicle traffic

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Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I.

21 January 2018

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SNAREpins: minimal machinery for membrane fusion

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SNARE complex formation is triggered by Ca2+ and drives membrane fusion

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The tandem C2 domains of synaptotagmin contain redundant Ca2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis.

21 January 2018

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Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis

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Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers

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Ca2+ regulates the interaction between synaptotagmin and syntaxin 1.

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The C2B domain of synaptotagmin I is a Ca2+-binding module

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Inhibition of neurotransmitter release by C2-domain peptides implicates synaptotagmin in exocytosis

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Postfusional regulation of cleft glutamate concentration during LTP at 'silent synapses'.

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synaptotagmin mutants reveal essential functions for the C2B domain in Ca2+-triggered fusion and recycling of synaptic vesicles in vivo

31 March 2020

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Structure/function analysis of Ca2+ binding to the C2A domain of synaptotagmin 1

31 March 2020

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Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I

31 March 2020

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Kinetics of synaptotagmin responses to Ca2+ and assembly with the core SNARE complex onto membranes

31 March 2020

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Membrane-embedded synaptotagmin penetrates cis or trans target membranes and clusters via a novel mechanism

31 March 2020

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The C2 domains of Rabphilin3A specifically bind phosphatidylinositol 4,5-bisphosphate containing vesicles in a Ca2+-dependent manner. In vitro characteristics and possible significance

31 March 2020

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Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a nonadditive manner

31 March 2020

1 reference

An essential role for a small synaptic vesicle-associated phosphatidylinositol 4-kinase in neurotransmitter release

31 March 2020

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Newly synthesized phosphatidylinositol phosphates are required for synaptic norepinephrine but not glutamate or gamma-aminobutyric acid (GABA) release

31 March 2020

1 reference

31 March 2020

Identifiers

DOI

10.1038/NSMB709

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16 June 2018

Dimensions Publication ID

1034327295

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16 June 2018