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Regional Specializations of the PAZ Proteomes Derived from Mouse Hippocampus, Olfactory Bulb and Cerebellum

Neurotransmitter release as well as structural and functional dynamics at the presynaptic active zone (PAZ) comprising synaptic vesicles attached to the presynaptic plasma membrane are mediated and controlled by its proteinaceous components. Here we describe a novel experimental design to immunopuri...

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Autores principales: Weingarten, Jens, Laßek, Melanie, Mueller, Benjamin F., Rohmer, Marion, Baeumlisberger, Dominic, Beckert, Benedikt, Ade, Jens, Gogesch, Patricia, Acker-Palmer, Amparo, Karas, Michael, Volknandt, Walter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5217373/
https://www.ncbi.nlm.nih.gov/pubmed/28248263
http://dx.doi.org/10.3390/proteomes3020074
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author Weingarten, Jens
Laßek, Melanie
Mueller, Benjamin F.
Rohmer, Marion
Baeumlisberger, Dominic
Beckert, Benedikt
Ade, Jens
Gogesch, Patricia
Acker-Palmer, Amparo
Karas, Michael
Volknandt, Walter
author_facet Weingarten, Jens
Laßek, Melanie
Mueller, Benjamin F.
Rohmer, Marion
Baeumlisberger, Dominic
Beckert, Benedikt
Ade, Jens
Gogesch, Patricia
Acker-Palmer, Amparo
Karas, Michael
Volknandt, Walter
author_sort Weingarten, Jens
collection PubMed
description Neurotransmitter release as well as structural and functional dynamics at the presynaptic active zone (PAZ) comprising synaptic vesicles attached to the presynaptic plasma membrane are mediated and controlled by its proteinaceous components. Here we describe a novel experimental design to immunopurify the native PAZ-complex from individual mouse brain regions such as olfactory bulb, hippocampus, and cerebellum with high purity that is essential for comparing their proteome composition. Interestingly, quantitative immunodetection demonstrates significant differences in the abundance of prominent calcium-dependent PAZ constituents. Furthermore, we characterized the proteomes of the immunoisolated PAZ derived from the three brain regions by mass spectrometry. The proteomes of the release sites from the respective regions exhibited remarkable differences in the abundance of a large variety of PAZ constituents involved in various functional aspects of the release sites such as calcium homeostasis, synaptic plasticity and neurogenesis. On the one hand, our data support an identical core architecture of the PAZ for all brain regions and, on the other hand, demonstrate that the proteinaceous composition of their presynaptic active zones vary, suggesting that changes in abundance of individual proteins strengthen the ability of the release sites to adapt to specific functional requirements.
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spelling pubmed-52173732017-02-27 Regional Specializations of the PAZ Proteomes Derived from Mouse Hippocampus, Olfactory Bulb and Cerebellum Weingarten, Jens Laßek, Melanie Mueller, Benjamin F. Rohmer, Marion Baeumlisberger, Dominic Beckert, Benedikt Ade, Jens Gogesch, Patricia Acker-Palmer, Amparo Karas, Michael Volknandt, Walter Proteomes Article Neurotransmitter release as well as structural and functional dynamics at the presynaptic active zone (PAZ) comprising synaptic vesicles attached to the presynaptic plasma membrane are mediated and controlled by its proteinaceous components. Here we describe a novel experimental design to immunopurify the native PAZ-complex from individual mouse brain regions such as olfactory bulb, hippocampus, and cerebellum with high purity that is essential for comparing their proteome composition. Interestingly, quantitative immunodetection demonstrates significant differences in the abundance of prominent calcium-dependent PAZ constituents. Furthermore, we characterized the proteomes of the immunoisolated PAZ derived from the three brain regions by mass spectrometry. The proteomes of the release sites from the respective regions exhibited remarkable differences in the abundance of a large variety of PAZ constituents involved in various functional aspects of the release sites such as calcium homeostasis, synaptic plasticity and neurogenesis. On the one hand, our data support an identical core architecture of the PAZ for all brain regions and, on the other hand, demonstrate that the proteinaceous composition of their presynaptic active zones vary, suggesting that changes in abundance of individual proteins strengthen the ability of the release sites to adapt to specific functional requirements. MDPI 2015-05-13 /pmc/articles/PMC5217373/ /pubmed/28248263 http://dx.doi.org/10.3390/proteomes3020074 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Weingarten, Jens
Laßek, Melanie
Mueller, Benjamin F.
Rohmer, Marion
Baeumlisberger, Dominic
Beckert, Benedikt
Ade, Jens
Gogesch, Patricia
Acker-Palmer, Amparo
Karas, Michael
Volknandt, Walter
Regional Specializations of the PAZ Proteomes Derived from Mouse Hippocampus, Olfactory Bulb and Cerebellum
title Regional Specializations of the PAZ Proteomes Derived from Mouse Hippocampus, Olfactory Bulb and Cerebellum
title_full Regional Specializations of the PAZ Proteomes Derived from Mouse Hippocampus, Olfactory Bulb and Cerebellum
title_fullStr Regional Specializations of the PAZ Proteomes Derived from Mouse Hippocampus, Olfactory Bulb and Cerebellum
title_full_unstemmed Regional Specializations of the PAZ Proteomes Derived from Mouse Hippocampus, Olfactory Bulb and Cerebellum
title_short Regional Specializations of the PAZ Proteomes Derived from Mouse Hippocampus, Olfactory Bulb and Cerebellum
title_sort regional specializations of the paz proteomes derived from mouse hippocampus, olfactory bulb and cerebellum
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5217373/
https://www.ncbi.nlm.nih.gov/pubmed/28248263
http://dx.doi.org/10.3390/proteomes3020074
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