Control of autophagosome axonal retrograde flux by presynaptic activity unveiled using botulinum neurotoxin type a.
Identifieur interne : 002E35 ( PubMed/Corpus ); précédent : 002E34; suivant : 002E36Control of autophagosome axonal retrograde flux by presynaptic activity unveiled using botulinum neurotoxin type a.
Auteurs : Tong Wang ; Sally Martin ; Andreas Papadopulos ; Callista B. Harper ; Timur A. Mavlyutov ; Dhevahi Niranjan ; Nick R. Glass ; Justin J. Cooper-White ; Jean-Baptiste Sibarita ; Daniel Choquet ; Bazbek Davletov ; Frédéric A. MeunierSource :
- The Journal of neuroscience : the official journal of the Society for Neuroscience [ 1529-2401 ] ; 2015.
English descriptors
- KwdEn :
- Androstadienes (pharmacology), Animals, Animals, Newborn, Autophagy (drug effects), Autophagy (physiology), Axonal Transport (drug effects), Axonal Transport (physiology), Botulinum Toxins, Type A (metabolism), Botulinum Toxins, Type A (pharmacology), Cells, Cultured, Enzyme Inhibitors (pharmacology), Female, Hippocampus (cytology), In Vitro Techniques, Macrolides (pharmacology), Male, Mice, Mice, Inbred C57BL, Microtubule-Associated Proteins (metabolism), Neurons (cytology), Neurons (drug effects), Neurons (ultrastructure), Neurotoxins (metabolism), Neurotoxins (pharmacology), Organ Culture Techniques, Rats, Rats, Sprague-Dawley, Receptors, Nerve Growth Factor (metabolism), Synaptosomal-Associated Protein 25 (metabolism).
- MESH :
- chemical , metabolism : Botulinum Toxins, Type A, Microtubule-Associated Proteins, Neurotoxins, Receptors, Nerve Growth Factor, Synaptosomal-Associated Protein 25.
- chemical , pharmacology : Androstadienes, Botulinum Toxins, Type A, Enzyme Inhibitors, Macrolides, Neurotoxins.
- cytology : Hippocampus, Neurons.
- drug effects : Autophagy, Axonal Transport, Neurons.
- physiology : Autophagy, Axonal Transport.
- ultrastructure : Neurons.
- Animals, Animals, Newborn, Cells, Cultured, Female, In Vitro Techniques, Male, Mice, Mice, Inbred C57BL, Organ Culture Techniques, Rats, Rats, Sprague-Dawley.
Abstract
Botulinum neurotoxin type A (BoNT/A) is a highly potent neurotoxin that elicits flaccid paralysis by enzymatic cleavage of the exocytic machinery component SNAP25 in motor nerve terminals. However, recent evidence suggests that the neurotoxic activity of BoNT/A is not restricted to the periphery, but also reaches the CNS after retrograde axonal transport. Because BoNT/A is internalized in recycling synaptic vesicles, it is unclear which compartment facilitates this transport. Using live-cell confocal and single-molecule imaging of rat hippocampal neurons cultured in microfluidic devices, we show that the activity-dependent uptake of the binding domain of the BoNT/A heavy chain (BoNT/A-Hc) is followed by a delayed increase in retrograde axonal transport of BoNT/A-Hc carriers. Consistent with a role of presynaptic activity in initiating transport of the active toxin, activity-dependent uptake of BoNT/A in the terminal led to a significant increase in SNAP25 cleavage detected in the soma chamber compared with nonstimulated neurons. Surprisingly, most endocytosed BoNT/A-Hc was incorporated into LC3-positive autophagosomes generated in the nerve terminals, which then underwent retrograde transport to the cell soma, where they fused with lysosomes both in vitro and in vivo. Blocking autophagosome formation or acidification with wortmannin or bafilomycin A1, respectively, inhibited the activity-dependent retrograde trafficking of BoNT/A-Hc. Our data demonstrate that both the presynaptic formation of autophagosomes and the initiation of their retrograde trafficking are tightly regulated by presynaptic activity.
DOI: 10.1523/JNEUROSCI.3757-14.2015
PubMed: 25878289
Links to Exploration step
pubmed:25878289Le document en format XML
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Harper</name><affiliation><nlm:affiliation>Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute.</nlm:affiliation></affiliation></author><author><name sortKey="Mavlyutov, Timur A" sort="Mavlyutov, Timur A" uniqKey="Mavlyutov T" first="Timur A" last="Mavlyutov">Timur A. Mavlyutov</name><affiliation><nlm:affiliation>University of Wisconsin Medical School, Madison, Wisconsin 53706.</nlm:affiliation></affiliation></author><author><name sortKey="Niranjan, Dhevahi" sort="Niranjan, Dhevahi" uniqKey="Niranjan D" first="Dhevahi" last="Niranjan">Dhevahi Niranjan</name><affiliation><nlm:affiliation>Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.</nlm:affiliation></affiliation></author><author><name sortKey="Glass, Nick R" sort="Glass, Nick R" uniqKey="Glass N" first="Nick R" last="Glass">Nick R. 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Cooper-White</name><affiliation><nlm:affiliation>Australian Institute for Bioengineering and Nanotechnology, and School of Chemical Engineering, University of Queensland, Brisbane, Queensland 4072, Australia, Materials Science and Engineering Division, Commonwealth Scientific and Industrial Research Organization, Clayton, Victoria 3169, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Sibarita, Jean Baptiste" sort="Sibarita, Jean Baptiste" uniqKey="Sibarita J" first="Jean-Baptiste" last="Sibarita">Jean-Baptiste Sibarita</name><affiliation><nlm:affiliation>University of Bordeaux, Interdisciplinary Institute for Neuroscience, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5297, Bordeaux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Choquet, Daniel" sort="Choquet, Daniel" uniqKey="Choquet D" first="Daniel" last="Choquet">Daniel Choquet</name><affiliation><nlm:affiliation>University of Bordeaux, Interdisciplinary Institute for Neuroscience, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5297, Bordeaux, France, Bordeaux Imaging Center, Unité Mixte de Service 3420, Centre National de la Recherche Scientifique, US4 INSERM, University of Bordeaux, France, and.</nlm:affiliation></affiliation></author><author><name sortKey="Davletov, Bazbek" sort="Davletov, Bazbek" uniqKey="Davletov B" first="Bazbek" last="Davletov">Bazbek Davletov</name><affiliation><nlm:affiliation>Department of Biomedical Science, The University of Sheffield, Sheffield, S10 2TN, United Kingdom.</nlm:affiliation></affiliation></author><author><name sortKey="Meunier, Frederic A" sort="Meunier, Frederic A" uniqKey="Meunier F" first="Frédéric A" last="Meunier">Frédéric A. Meunier</name><affiliation><nlm:affiliation>Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, f.meunier@uq.edu.au.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The Journal of neuroscience : the official journal of the Society for Neuroscience</title><idno type="eISSN">1529-2401</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Androstadienes (pharmacology)</term><term>Animals</term><term>Animals, Newborn</term><term>Autophagy (drug effects)</term><term>Autophagy (physiology)</term><term>Axonal Transport (drug effects)</term><term>Axonal Transport (physiology)</term><term>Botulinum Toxins, Type A (metabolism)</term><term>Botulinum Toxins, Type A (pharmacology)</term><term>Cells, Cultured</term><term>Enzyme Inhibitors (pharmacology)</term><term>Female</term><term>Hippocampus (cytology)</term><term>In Vitro Techniques</term><term>Macrolides (pharmacology)</term><term>Male</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Microtubule-Associated Proteins (metabolism)</term><term>Neurons (cytology)</term><term>Neurons (drug effects)</term><term>Neurons (ultrastructure)</term><term>Neurotoxins (metabolism)</term><term>Neurotoxins (pharmacology)</term><term>Organ Culture Techniques</term><term>Rats</term><term>Rats, Sprague-Dawley</term><term>Receptors, Nerve Growth Factor (metabolism)</term><term>Synaptosomal-Associated Protein 25 (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Botulinum Toxins, Type A</term><term>Microtubule-Associated Proteins</term><term>Neurotoxins</term><term>Receptors, Nerve Growth Factor</term><term>Synaptosomal-Associated Protein 25</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Androstadienes</term><term>Botulinum Toxins, Type A</term><term>Enzyme Inhibitors</term><term>Macrolides</term><term>Neurotoxins</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Hippocampus</term><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term><term>Axonal Transport</term><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Autophagy</term><term>Axonal Transport</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Neurons</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Animals, Newborn</term><term>Cells, Cultured</term><term>Female</term><term>In Vitro Techniques</term><term>Male</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Organ Culture Techniques</term><term>Rats</term><term>Rats, Sprague-Dawley</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Botulinum neurotoxin type A (BoNT/A) is a highly potent neurotoxin that elicits flaccid paralysis by enzymatic cleavage of the exocytic machinery component SNAP25 in motor nerve terminals. However, recent evidence suggests that the neurotoxic activity of BoNT/A is not restricted to the periphery, but also reaches the CNS after retrograde axonal transport. Because BoNT/A is internalized in recycling synaptic vesicles, it is unclear which compartment facilitates this transport. Using live-cell confocal and single-molecule imaging of rat hippocampal neurons cultured in microfluidic devices, we show that the activity-dependent uptake of the binding domain of the BoNT/A heavy chain (BoNT/A-Hc) is followed by a delayed increase in retrograde axonal transport of BoNT/A-Hc carriers. Consistent with a role of presynaptic activity in initiating transport of the active toxin, activity-dependent uptake of BoNT/A in the terminal led to a significant increase in SNAP25 cleavage detected in the soma chamber compared with nonstimulated neurons. Surprisingly, most endocytosed BoNT/A-Hc was incorporated into LC3-positive autophagosomes generated in the nerve terminals, which then underwent retrograde transport to the cell soma, where they fused with lysosomes both in vitro and in vivo. Blocking autophagosome formation or acidification with wortmannin or bafilomycin A1, respectively, inhibited the activity-dependent retrograde trafficking of BoNT/A-Hc. Our data demonstrate that both the presynaptic formation of autophagosomes and the initiation of their retrograde trafficking are tightly regulated by presynaptic activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25878289</PMID><DateCreated><Year>2015</Year><Month>04</Month><Day>16</Day></DateCreated><DateCompleted><Year>2015</Year><Month>06</Month><Day>18</Day></DateCompleted><DateRevised><Year>2017</Year><Month>09</Month><Day>22</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1529-2401</ISSN><JournalIssue CitedMedium="Internet"><Volume>35</Volume><Issue>15</Issue><PubDate><Year>2015</Year><Month>Apr</Month><Day>15</Day></PubDate></JournalIssue><Title>The Journal of neuroscience : the official journal of the Society for Neuroscience</Title><ISOAbbreviation>J. Neurosci.</ISOAbbreviation></Journal><ArticleTitle>Control of autophagosome axonal retrograde flux by presynaptic activity unveiled using botulinum neurotoxin type a.</ArticleTitle><Pagination><MedlinePgn>6179-94</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1523/JNEUROSCI.3757-14.2015</ELocationID><Abstract><AbstractText>Botulinum neurotoxin type A (BoNT/A) is a highly potent neurotoxin that elicits flaccid paralysis by enzymatic cleavage of the exocytic machinery component SNAP25 in motor nerve terminals. However, recent evidence suggests that the neurotoxic activity of BoNT/A is not restricted to the periphery, but also reaches the CNS after retrograde axonal transport. Because BoNT/A is internalized in recycling synaptic vesicles, it is unclear which compartment facilitates this transport. Using live-cell confocal and single-molecule imaging of rat hippocampal neurons cultured in microfluidic devices, we show that the activity-dependent uptake of the binding domain of the BoNT/A heavy chain (BoNT/A-Hc) is followed by a delayed increase in retrograde axonal transport of BoNT/A-Hc carriers. Consistent with a role of presynaptic activity in initiating transport of the active toxin, activity-dependent uptake of BoNT/A in the terminal led to a significant increase in SNAP25 cleavage detected in the soma chamber compared with nonstimulated neurons. Surprisingly, most endocytosed BoNT/A-Hc was incorporated into LC3-positive autophagosomes generated in the nerve terminals, which then underwent retrograde transport to the cell soma, where they fused with lysosomes both in vitro and in vivo. Blocking autophagosome formation or acidification with wortmannin or bafilomycin A1, respectively, inhibited the activity-dependent retrograde trafficking of BoNT/A-Hc. Our data demonstrate that both the presynaptic formation of autophagosomes and the initiation of their retrograde trafficking are tightly regulated by presynaptic activity.</AbstractText><CopyrightInformation>Copyright © 2015 the authors 0270-6474/15/356179-16$15.00/0.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Tong</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martin</LastName><ForeName>Sally</ForeName><Initials>S</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-9294-5404</Identifier><AffiliationInfo><Affiliation>Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Papadopulos</LastName><ForeName>Andreas</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Harper</LastName><ForeName>Callista B</ForeName><Initials>CB</Initials><AffiliationInfo><Affiliation>Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mavlyutov</LastName><ForeName>Timur A</ForeName><Initials>TA</Initials><AffiliationInfo><Affiliation>University of Wisconsin Medical School, Madison, Wisconsin 53706.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Niranjan</LastName><ForeName>Dhevahi</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Glass</LastName><ForeName>Nick R</ForeName><Initials>NR</Initials><AffiliationInfo><Affiliation>Australian Institute for Bioengineering and Nanotechnology, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cooper-White</LastName><ForeName>Justin J</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>Australian Institute for Bioengineering and Nanotechnology, and School of Chemical Engineering, University of Queensland, Brisbane, Queensland 4072, Australia, Materials Science and Engineering Division, Commonwealth Scientific and Industrial Research Organization, Clayton, Victoria 3169, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sibarita</LastName><ForeName>Jean-Baptiste</ForeName><Initials>JB</Initials><AffiliationInfo><Affiliation>University of Bordeaux, Interdisciplinary Institute for Neuroscience, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5297, Bordeaux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Choquet</LastName><ForeName>Daniel</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>University of Bordeaux, Interdisciplinary Institute for Neuroscience, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5297, Bordeaux, France, Bordeaux Imaging Center, Unité Mixte de Service 3420, Centre National de la Recherche Scientifique, US4 INSERM, University of Bordeaux, France, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Davletov</LastName><ForeName>Bazbek</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Biomedical Science, The University of Sheffield, Sheffield, S10 2TN, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Meunier</LastName><ForeName>Frédéric A</ForeName><Initials>FA</Initials><AffiliationInfo><Affiliation>Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, f.meunier@uq.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>MC_U105178791</GrantID><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>MR/K022539/1</GrantID><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Neurosci</MedlineTA><NlmUniqueID>8102140</NlmUniqueID><ISSNLinking>0270-6474</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000730">Androstadienes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme 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UI="C040929">bafilomycin A1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.69</RegistryNumber><NameOfSubstance UI="D019274">Botulinum Toxins, Type A</NameOfSubstance></Chemical><Chemical><RegistryNumber>XVA4O219QW</RegistryNumber><NameOfSubstance UI="C009687">wortmannin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Eur J Biochem. 1997 Jan 15;243(1-2):240-6</RefSource><PMID Version="1">9030745</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Microbiology. 1997 Oct;143 ( Pt 10):3337-47</RefSource><PMID Version="1">9353935</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Cell Struct Funct. 1998 Feb;23(1):33-42</RefSource><PMID Version="1">9639028</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>FEBS Lett. 2006 Apr 3;580(8):2011-4</RefSource><PMID 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