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  • 1.
    Farsi, Zohreh
    et al.
    Max Planck Inst Biophys Chem, Dept Neurobiol, Gottingen, Germany.;Max Delbruck Ctr Mol Med, Berlin Inst Med Syst Biol, Berlin, Germany..
    Gowrisankaran, Sindhuja
    Univ Med Ctr Gottingen, European Neurosci Inst, Synapt Vesicle Dynam Grp, Gottingen, Germany..
    Krunic, Matija
    Univ Med Ctr Gottingen, European Neurosci Inst, Synapt Vesicle Dynam Grp, Gottingen, Germany..
    Rammner, Burkhard
    Sciloop, Hamburg, Germany..
    Woehler, Andrew
    Max Delbruck Ctr Mol Med, Berlin Inst Med Syst Biol, Berlin, Germany..
    Lafer, Eileen M.
    Univ Texas Hlth Sci Ctr San Antonio, Dept Biochem & Struct Biol, San Antonio, TX 78229 USA.;Univ Texas Hlth Sci Ctr San Antonio, Ctr Biomed Neurosci, San Antonio, TX 78229 USA..
    Mim, Carsten
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Biomedical Engineering and Health Systems.
    Jahn, Reinhard
    Max Planck Inst Biophys Chem, Dept Neurobiol, Gottingen, Germany..
    Milosevic, Ira
    Univ Med Ctr Gottingen, European Neurosci Inst, Synapt Vesicle Dynam Grp, Gottingen, Germany..
    Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity2018In: eLIFE, E-ISSN 2050-084X, Vol. 7, article id e32569Article in journal (Refereed)
    Abstract [en]

    Newly-formed synaptic vesicles (SVs) are rapidly acidified by vacuolar adenosine triphosphatases (vATPases), generating a proton electrochemical gradient that drives neurotransmitter loading. Clathrin-mediated endocytosis is needed for the formation of new SVs, yet it is unclear when endocytosed vesicles acidify and refill at the synapse. Here, we isolated clathrin-coated vesicles (CCVs) from mouse brain to measure their acidification directly at the single vesicle level. We observed that the ATP-induced acidification of CCVs was strikingly reduced in comparison to SVs. Remarkably, when the coat was removed from CCVs, uncoated vesicles regained ATP-dependent acidification, demonstrating that CCVs contain the functional vATPase, yet its function is inhibited by the clathrin coat. Considering the known structures of the vATPase and clathrin coat, we propose a model in which the formation of the coat surrounds the vATPase and blocks its activity. Such inhibition is likely fundamental for the proper timing of SV refilling.

  • 2.
    Farsi, Zohreh
    et al.
    Helmholtz Assoc, Max Delbruck Ctr Mol Med, Light Microscopy Platform, Berlin, Germany..
    Gowrisankaran, Sindhuja
    European Neurosci Inst, Gottingen, Germany..
    Krunic, Matija
    European Neurosci Inst, Gottingen, Germany..
    Rammner, Burkhard
    Sciloop, Hamburg, Germany..
    Woehler, Andrew
    Helmholtz Assoc, Max Delbruck Ctr Mol Med, Light Microscopy Platform, Berlin, Germany..
    Mim, Carsten
    KTH, School of Technology and Health (STH).
    Jahn, Reinhard
    Max Planck Inst Biophys Chem, Neurobiol, Gottingen, Germany..
    Milosevic, Ira
    European Neurosci Inst, Synapt Vesicle Dynam, Gottingen, Germany..
    Clathrin Coat Controls Vesicle Acidification by Blocking Vacuolar ATPase Activity2018In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 114, no 3, p. 280A-280AArticle in journal (Other academic)
  • 3.
    Sporny, Michael
    et al.
    Bar Ilan Univ, Mina & Everard Goodman Fac Life Sci, IL-5290002 Ramat Gan, Israel..
    Guez-Haddad, Julia
    Bar Ilan Univ, Mina & Everard Goodman Fac Life Sci, IL-5290002 Ramat Gan, Israel..
    Lebendiker, Mario
    Hebrew Univ Jerusalem, Wolfson Ctr Appl Struct Biol, Jerusalem, Israel..
    Ulisse, Valeria
    Weizmann Inst Sci, Dept Biomol Sci, Rehovot, Israel..
    Volf, Allison
    Bar Ilan Univ, Mina & Everard Goodman Fac Life Sci, IL-5290002 Ramat Gan, Israel..
    Mim, Carsten
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Biomedical Engineering and Health Systems, Structural Biotechnology. Karolinska Inst, Dept Nutr & Biosci, Huddinge, Sweden..
    Isupov, Michail N.
    Univ Exeter, Biosci, Exeter, Devon, England..
    Opatowsky, Yarden
    Bar Ilan Univ, Mina & Everard Goodman Fac Life Sci, IL-5290002 Ramat Gan, Israel..
    Structural Evidence for an Octameric Ring Arrangement of SARM12019In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 431, no 19, p. 3591-3605Article in journal (Refereed)
    Abstract [en]

    SARM1 induces axonal degeneration in response to various insults and is therefore considered an attractive drug target for the treatment of neuro-degenerative diseases as well as for brain and spinal cord injuries. SARM1 activity depends on the integrity of the protein's SAM domains, as well as on the enzymatic conversion of NAD + to ADPR (ADP Ribose) products by the SARM1's TIR domain. Therefore, inhibition of either SAM or TIR functions may constitute an effective therapeutic strategy. However, there is currently no SARM1-directed therapeutic approach available because of an insufficient structural and mechanistic understanding of this protein. In this study, we found that SARM1 assembles into an octameric ring. This arrangement was not described before in other SAM proteins, but is reminiscent of the apoptosome and inflammasome well-known apoptotic ring-like oligomers. We show that both SARM1 and the isolated tandem SAM(1-2) domains form octamers in solution, and electron microscopy analysis reveals an octameric ring of SARM1. We determined the crystal structure of SAM(1-2) and found that it also forms a closed octameric ring in the crystal lattice. The SAM(1-2) ring interactions are mediated by complementing "lock and key" hydrophobic grooves and inserts and electrostatic charges between the neighboring protomers. We have mutated several interacting SAM1-2 interfaces and measured how these mutations affect SARM1 apoptotic activity in cultured cells, and in this way identified critical oligomerization sites that facilitate cell death. These results highlight the importance of oligomerization for SARM1 function and reveal critical epitopes for future targeted drug development. Elsevier Ltd. All rights reserved.

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