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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<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>
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<ArticleTitle>Control of autophagosome axonal retrograde flux by presynaptic activity unveiled using botulinum neurotoxin type a.</ArticleTitle>
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<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>
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<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 Version="1">16545378</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Science. 2006 Apr 28;312(5773):592-6</RefSource>
<PMID Version="1">16543415</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2006 Aug 2;26(31):8057-68</RefSource>
<PMID Version="1">16885219</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Traffic. 2007 Feb;8(2):142-53</RefSource>
<PMID Version="1">17241445</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Autophagy. 2007 Sep-Oct;3(5):452-60</RefSource>
<PMID Version="1">17534139</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Cell Biol. 2007 Oct;9(10):1102-9</RefSource>
<PMID Version="1">17909521</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2008 Apr 2;28(14):3689-96</RefSource>
<PMID Version="1">18385327</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Methods Mol Biol. 2008;445:77-88</RefSource>
<PMID Version="1">18425443</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Biol Cell. 2008 Dec;19(12):5593-603</RefSource>
<PMID Version="1">18843041</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Cell Death Differ. 2009 Jan;16(1):70-8</RefSource>
<PMID Version="1">19008921</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 2014 Jan 2;505(7481):108-11</RefSource>
<PMID Version="1">24240280</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Autophagy. 2010 Apr;6(3):378-85</RefSource>
<PMID Version="1">20150763</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2011 May 25;31(21):7817-30</RefSource>
<PMID Version="1">21613495</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Annu Rev Biochem. 2011;80:125-56</RefSource>
<PMID Version="1">21548784</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Dev Cell. 2011 Sep 13;21(3):431-44</RefSource>
<PMID Version="1">21856246</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Commun. 2011;2:491</RefSource>
<PMID Version="1">21971506</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2011 Oct 14;286(41):35966-76</RefSource>
<PMID Version="1">21832053</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2011 Nov 2;31(44):15650-9</RefSource>
<PMID Version="1">22049408</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 2012 Feb 20;196(4):407-17</RefSource>
<PMID Version="1">22331844</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2012 Jul 25;32(30):10413-22</RefSource>
<PMID Version="1">22836274</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Autophagy. 2012 May 1;8(5):858-60</RefSource>
<PMID Version="1">22617438</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS Pathog. 2012 Dec;8(12):e1003087</RefSource>
<PMID Version="1">23300443</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2013;8(3):e60152</RefSource>
<PMID Version="1">23544129</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2013 Apr 19;288(16):11144-54</RefSource>
<PMID Version="1">23471969</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2013;8(4):e62918</RefSource>
<PMID Version="1">23646160</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Trends Neurosci. 2013 Jul;36(7):418-28</RefSource>
<PMID Version="1">23639383</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Neurobiol. 2013 Aug;48(1):120-7</RefSource>
<PMID Version="1">23471747</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Med. 2013 Aug;19(8):983-97</RefSource>
<PMID Version="1">23921753</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2013 Aug 7;33(32):13204-24</RefSource>
<PMID Version="1">23926273</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2013 Dec 4;33(49):19143-53</RefSource>
<PMID Version="1">24305811</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1998 Aug 21;273(34):21883-92</RefSource>
<PMID Version="1">9705327</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biophys J. 1999 Apr;76(4):2262-71</RefSource>
<PMID Version="1">10096921</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Philos Trans R Soc Lond B Biol Sci. 1999 Feb 28;354(1381):259-68</RefSource>
<PMID Version="1">10212474</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurocytol. 1998 Aug;27(8):559-73</RefSource>
<PMID Version="1">10405023</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO Rep. 2004 Nov;5(11):1090-5</RefSource>
<PMID Version="1">15486565</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochem Soc Symp. 2005;(72):139-50</RefSource>
<PMID Version="1">15649138</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 2005 May 9;169(3):425-34</RefSource>
<PMID Version="1">15866887</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Rev Neurosci. 2005 Aug;6(8):615-25</RefSource>
<PMID Version="1">16062170</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Methods. 2005 Aug;2(8):599-605</RefSource>
<PMID Version="1">16094385</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Biol Cell. 2005 Oct;16(10):4841-51</RefSource>
<PMID Version="1">16055506</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2014;9(1):e87242</RefSource>
<PMID Version="1">24489879</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Rev Microbiol. 2014 Aug;12(8):535-49</RefSource>
<PMID Version="1">24975322</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS Pathog. 2014 Aug;10(8):e1004348</RefSource>
<PMID Version="1">25165859</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Cell Rep. 2014 Sep 25;8(6):1870-8</RefSource>
<PMID Version="1">25220457</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Cell Microbiol. 2009 Feb;11(2):289-308</RefSource>
<PMID Version="1">19016790</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2009 Apr;109(1):15-24</RefSource>
<PMID Version="1">19154335</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 2009 Jun 23;48(24):5631-41</RefSource>
<PMID Version="1">19476346</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Physiol Rev. 2000 Apr;80(2):717-66</RefSource>
<PMID Version="1">10747206</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2000 Nov 1;19(21):5720-8</RefSource>
<PMID Version="1">11060023</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 2001 Feb 19;152(4):657-68</RefSource>
<PMID Version="1">11266458</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Physiol Paris. 2002 Jan-Mar;96(1-2):105-13</RefSource>
<PMID Version="1">11755789</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 2002 Jan 21;156(2):233-9</RefSource>
<PMID Version="1">11807088</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Struct Biol. 2003 Jan;10(1):13-8</RefSource>
<PMID Version="1">12459720</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2003 Apr 15;23(8):3209-20</RefSource>
<PMID Version="1">12716928</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Cell Neurosci. 2003 Apr;22(4):454-66</RefSource>
<PMID Version="1">12727443</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Trends Mol Med. 2003 Jul;9(7):291-9</RefSource>
<PMID Version="1">12900216</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurobiol. 2004 Feb 5;58(2):295-314</RefSource>
<PMID Version="1">14704960</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2004 Apr 21;24(16):3907-16</RefSource>
<PMID Version="1">15102906</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 1984 Feb 2-8;307(5950):457-60</RefSource>
<PMID Version="1">6694738</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1990 Jun 5;265(16):9153-8</RefSource>
<PMID Version="1">2160960</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 1992 Oct;119(1):123-37</RefSource>
<PMID Version="1">1527164</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 1993 Sep 9;365(6442):160-3</RefSource>
<PMID Version="1">8103915</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>FEBS Lett. 1993 Nov 29;335(1):99-103</RefSource>
<PMID Version="1">8243676</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Histochemistry. 1994 Nov;102(5):329-35</RefSource>
<PMID Version="1">7868367</PMID>
</CommentsCorrections>
</CommentsCorrectionsList>
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