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SynProt: A Database for Proteins of Detergent-Resistant Synaptic Protein Preparations

Chemical synapses are highly specialized cell–cell contacts for communication between neurons in the CNS characterized by complex and dynamic protein networks at both synaptic membranes. The cytomatrix at the active zone (CAZ) organizes the apparatus for the regulated release of transmitters from th...

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Autores principales: Pielot, Rainer, Smalla, Karl-Heinz, Müller, Anke, Landgraf, Peter, Lehmann, Anne-Christin, Eisenschmidt, Elke, Haus, Utz-Uwe, Weismantel, Robert, Gundelfinger, Eckart D., Dieterich, Daniela C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Research Foundation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3382120/
https://www.ncbi.nlm.nih.gov/pubmed/22737123
http://dx.doi.org/10.3389/fnsyn.2012.00001
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author Pielot, Rainer
Smalla, Karl-Heinz
Müller, Anke
Landgraf, Peter
Lehmann, Anne-Christin
Eisenschmidt, Elke
Haus, Utz-Uwe
Weismantel, Robert
Gundelfinger, Eckart D.
Dieterich, Daniela C.
author_facet Pielot, Rainer
Smalla, Karl-Heinz
Müller, Anke
Landgraf, Peter
Lehmann, Anne-Christin
Eisenschmidt, Elke
Haus, Utz-Uwe
Weismantel, Robert
Gundelfinger, Eckart D.
Dieterich, Daniela C.
author_sort Pielot, Rainer
collection PubMed
description Chemical synapses are highly specialized cell–cell contacts for communication between neurons in the CNS characterized by complex and dynamic protein networks at both synaptic membranes. The cytomatrix at the active zone (CAZ) organizes the apparatus for the regulated release of transmitters from the presynapse. At the postsynaptic side, the postsynaptic density constitutes the machinery for detection, integration, and transduction of the transmitter signal. Both pre- and postsynaptic protein networks represent the molecular substrates for synaptic plasticity. Their function can be altered both by regulating their composition and by post-translational modification of their components. For a comprehensive understanding of synaptic networks the entire ensemble of synaptic proteins has to be considered. To support this, we established a comprehensive database for synaptic junction proteins (SynProt database) primarily based on proteomics data obtained from biochemical preparations of detergent-resistant synaptic junctions. The database currently contains 2,788 non-redundant entries of rat, mouse, and some human proteins, which mainly have been manually extracted from 12 proteomic studies and annotated for synaptic subcellular localization. Each dataset is completed with manually added information including protein classifiers as well as automatically retrieved and updated information from public databases (UniProt and PubMed). We intend that the database will be used to support modeling of synaptic protein networks and rational experimental design.
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spelling pubmed-33821202012-06-26 SynProt: A Database for Proteins of Detergent-Resistant Synaptic Protein Preparations Pielot, Rainer Smalla, Karl-Heinz Müller, Anke Landgraf, Peter Lehmann, Anne-Christin Eisenschmidt, Elke Haus, Utz-Uwe Weismantel, Robert Gundelfinger, Eckart D. Dieterich, Daniela C. Front Synaptic Neurosci Neuroscience Chemical synapses are highly specialized cell–cell contacts for communication between neurons in the CNS characterized by complex and dynamic protein networks at both synaptic membranes. The cytomatrix at the active zone (CAZ) organizes the apparatus for the regulated release of transmitters from the presynapse. At the postsynaptic side, the postsynaptic density constitutes the machinery for detection, integration, and transduction of the transmitter signal. Both pre- and postsynaptic protein networks represent the molecular substrates for synaptic plasticity. Their function can be altered both by regulating their composition and by post-translational modification of their components. For a comprehensive understanding of synaptic networks the entire ensemble of synaptic proteins has to be considered. To support this, we established a comprehensive database for synaptic junction proteins (SynProt database) primarily based on proteomics data obtained from biochemical preparations of detergent-resistant synaptic junctions. The database currently contains 2,788 non-redundant entries of rat, mouse, and some human proteins, which mainly have been manually extracted from 12 proteomic studies and annotated for synaptic subcellular localization. Each dataset is completed with manually added information including protein classifiers as well as automatically retrieved and updated information from public databases (UniProt and PubMed). We intend that the database will be used to support modeling of synaptic protein networks and rational experimental design. Frontiers Research Foundation 2012-06-25 /pmc/articles/PMC3382120/ /pubmed/22737123 http://dx.doi.org/10.3389/fnsyn.2012.00001 Text en Copyright © 2012 Pielot, Smalla, Müller, Landgraf, Lehmann, Eisenschmidt, Haus, Weismantel, Gundelfinger and Dieterich. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited.
spellingShingle Neuroscience
Pielot, Rainer
Smalla, Karl-Heinz
Müller, Anke
Landgraf, Peter
Lehmann, Anne-Christin
Eisenschmidt, Elke
Haus, Utz-Uwe
Weismantel, Robert
Gundelfinger, Eckart D.
Dieterich, Daniela C.
SynProt: A Database for Proteins of Detergent-Resistant Synaptic Protein Preparations
title SynProt: A Database for Proteins of Detergent-Resistant Synaptic Protein Preparations
title_full SynProt: A Database for Proteins of Detergent-Resistant Synaptic Protein Preparations
title_fullStr SynProt: A Database for Proteins of Detergent-Resistant Synaptic Protein Preparations
title_full_unstemmed SynProt: A Database for Proteins of Detergent-Resistant Synaptic Protein Preparations
title_short SynProt: A Database for Proteins of Detergent-Resistant Synaptic Protein Preparations
title_sort synprot: a database for proteins of detergent-resistant synaptic protein preparations
topic Neuroscience
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3382120/
https://www.ncbi.nlm.nih.gov/pubmed/22737123
http://dx.doi.org/10.3389/fnsyn.2012.00001
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