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Synaptotagmin Interaction with the Syntaxin/SNAP-25 Dimer Is Mediated by an Evolutionarily Conserved Motif and Is Sensitive to Inositol Hexakisphosphate*

Overview of attention for article published in Journal of Biological Chemistry, January 2004
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2 Wikipedia pages

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109 Dimensions

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69 Mendeley
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Title
Synaptotagmin Interaction with the Syntaxin/SNAP-25 Dimer Is Mediated by an Evolutionarily Conserved Motif and Is Sensitive to Inositol Hexakisphosphate*
Published in
Journal of Biological Chemistry, January 2004
DOI 10.1074/jbc.m310710200
Pubmed ID
Authors

Colin Rickman, Deborah A. Archer, Frederic A. Meunier, Molly Craxton, Mitsunori Fukuda, Robert D. Burgoyne, Bazbek Davletov

Abstract

Synaptotagmins are membrane proteins that possess tandem C2 domains and play an important role in regulated membrane fusion in metazoan organisms. Here we show that both synaptotagmins I and II, the two major neuronal isoforms, can interact with the syntaxin/synaptosomal-associated protein of 25 kDa (SNAP-25) dimer, the immediate precursor of the soluble NSF attachment protein receptor (SNARE) fusion complex. A stretch of basic amino acids highly conserved throughout the animal kingdom is responsible for this calcium-independent interaction. Inositol hexakisphosphate modulates synaptotagmin coupling to the syntaxin/SNAP-25 dimer, which is mirrored by changes in chromaffin cell exocytosis. Our results shed new light on the functional importance of the conserved polybasic synaptotagmin motif, suggesting that synaptotagmin interacts with the t-SNARE dimer to up-regulate the probability of SNARE-mediated membrane fusion.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 69 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 4 6%
Japan 1 1%
United States 1 1%
Switzerland 1 1%
Unknown 62 90%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 21 30%
Researcher 14 20%
Professor > Associate Professor 8 12%
Student > Master 6 9%
Student > Bachelor 5 7%
Other 8 12%
Unknown 7 10%
Readers by discipline Count As %
Agricultural and Biological Sciences 33 48%
Biochemistry, Genetics and Molecular Biology 11 16%
Medicine and Dentistry 5 7%
Neuroscience 5 7%
Chemistry 3 4%
Other 4 6%
Unknown 8 12%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 July 2018.
All research outputs
#8,535,472
of 25,374,647 outputs
Outputs from Journal of Biological Chemistry
#32,957
of 85,240 outputs
Outputs of similar age
#37,356
of 146,134 outputs
Outputs of similar age from Journal of Biological Chemistry
#322
of 834 outputs
Altmetric has tracked 25,374,647 research outputs across all sources so far. This one is in the 43rd percentile – i.e., 43% of other outputs scored the same or lower than it.
So far Altmetric has tracked 85,240 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.1. This one is in the 15th percentile – i.e., 15% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 146,134 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 15th percentile – i.e., 15% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 834 others from the same source and published within six weeks on either side of this one. This one is in the 6th percentile – i.e., 6% of its contemporaries scored the same or lower than it.