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  1. Article: WHO'S WHO AT BIF? Prof. Dr rer. nat. Reinhard Jahn, member of BIF's Board of Trustees, answers the BIF Questionnaire

    Jahn, Reinhard

    Futura

    2011  Volume 26, Issue 1, Page(s) 41

    Language German ; English
    Document type Article
    ZDB-ID 382906-6
    ISSN 0179-6372
    Database Current Contents Medicine

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    Zs.B 2980: Show issues Location:
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  2. Article ; Online: Rab GTPases and phosphoinositides fine-tune SNAREs dependent targeting specificity of intracellular vesicle traffic.

    Koike, Seiichi / Jahn, Reinhard

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 2508

    Abstract: In the secretory pathway the destination of trafficking vesicles is determined by specific proteins that, with the notable exception of SNAREs, are recruited from soluble pools. Previously we have shown that microinjected proteoliposomes containing early ...

    Abstract In the secretory pathway the destination of trafficking vesicles is determined by specific proteins that, with the notable exception of SNAREs, are recruited from soluble pools. Previously we have shown that microinjected proteoliposomes containing early or late endosomal SNAREs, respectively, are targeted to the corresponding endogenous compartments, with targeting specificity being dependent on the recruitment of tethering factors by some of the SNAREs. Here, we show that targeting of SNARE-containing liposomes is refined upon inclusion of polyphosphoinositides and Rab5. Intriguingly, targeting specificity is dependent on the concentration of PtdIns(3)P, and on the recruitment of PtdIns(3)P binding proteins such as rabenosyn-5 and PIKfyve, with conversion of PtdIns(3)P into PtdIns(3,5)P2 re-routing the liposomes towards late endosomes despite the presence of GTP-Rab5 and early endosomal SNAREs. Our data reveal a complex interplay between permissive and inhibitory targeting signals that sharpen a basic targeting and fusion machinery for conveying selectivity in intracellular membrane traffic.
    MeSH term(s) SNARE Proteins/metabolism ; rab GTP-Binding Proteins/metabolism ; Phosphatidylinositols/metabolism ; Liposomes/metabolism ; Endosomes/metabolism ; Membrane Fusion
    Chemical Substances SNARE Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2) ; Phosphatidylinositols ; Liposomes
    Language English
    Publishing date 2024-03-20
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-46678-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: SNARE proteins: zip codes in vesicle targeting?

    Koike, Seiichi / Jahn, Reinhard

    The Biochemical journal

    2022  Volume 479, Issue 3, Page(s) 273–288

    Abstract: Membrane traffic in eukaryotic cells is mediated by transport vesicles that bud from a precursor compartment and are transported to their destination compartment where they dock and fuse. To reach their intracellular destination, transport vesicles ... ...

    Abstract Membrane traffic in eukaryotic cells is mediated by transport vesicles that bud from a precursor compartment and are transported to their destination compartment where they dock and fuse. To reach their intracellular destination, transport vesicles contain targeting signals such as Rab GTPases and polyphosphoinositides that are recognized by tethering factors in the cytoplasm and that connect the vesicles with their respective destination compartment. The final step, membrane fusion, is mediated by SNARE proteins. SNAREs are connected to targeting signals and tethering factors by multiple interactions. However, it is still debated whether SNAREs only function downstream of targeting and tethering or whether they also participate in regulating targeting specificity. Here, we review the evidence and discuss recent data supporting a role of SNARE proteins as targeting signals in vesicle traffic.
    MeSH term(s) Cell Membrane/metabolism ; Eukaryotic Cells/metabolism ; Humans ; Membrane Fusion/physiology ; Protein Transport/physiology ; SNARE Proteins/metabolism ; Signal Transduction/physiology ; Transport Vesicles/metabolism ; rab GTP-Binding Proteins/metabolism
    Chemical Substances SNARE Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2022-02-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20210719
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Mechanisms of SNARE proteins in membrane fusion.

    Jahn, Reinhard / Cafiso, David C / Tamm, Lukas K

    Nature reviews. Molecular cell biology

    2023  Volume 25, Issue 2, Page(s) 101–118

    Abstract: Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are a family of small conserved eukaryotic proteins that mediate membrane fusion between organelles and with the plasma membrane. SNAREs are directly or indirectly anchored ... ...

    Abstract Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are a family of small conserved eukaryotic proteins that mediate membrane fusion between organelles and with the plasma membrane. SNAREs are directly or indirectly anchored to membranes. Prior to fusion, complementary SNAREs assemble between membranes with the aid of accessory proteins that provide a scaffold to initiate SNARE zippering, pulling the membranes together and mediating fusion. Recent advances have enabled the construction of detailed models describing bilayer transitions and energy barriers along the fusion pathway and have elucidated the structures of SNAREs complexed in various states with regulatory proteins. In this Review, we discuss how these advances are yielding an increasingly detailed picture of the SNARE-mediated fusion pathway, leading from first contact between the membranes via metastable non-bilayer intermediates towards the opening and expansion of a fusion pore. We describe how SNARE proteins assemble into complexes, how this assembly is regulated by accessory proteins and how SNARE complexes overcome the free energy barriers that prevent spontaneous membrane fusion.
    MeSH term(s) SNARE Proteins ; Membrane Fusion ; Cell Membrane/metabolism
    Chemical Substances SNARE Proteins
    Language English
    Publishing date 2023-10-17
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/s41580-023-00668-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5446: Show issues Location:
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    Zs.MG 26: Show issues

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  5. Article ; Online: All SNAP25 molecules in the vesicle-plasma membrane contact zone change conformation during vesicle priming.

    Zhao, Ying / Fang, Qinghua / Sharma, Satyan / Jakhanwal, Shrutee / Jahn, Reinhard / Lindau, Manfred

    Proceedings of the National Academy of Sciences of the United States of America

    2024  Volume 121, Issue 2, Page(s) e2309161121

    Abstract: In neuronal cell types, vesicular exocytosis is governed by the SNARE (soluble NSF attachment receptor) complex consisting of synaptobrevin2, SNAP25, and syntaxin1. These proteins are required for vesicle priming and fusion. We generated an improved ... ...

    Abstract In neuronal cell types, vesicular exocytosis is governed by the SNARE (soluble NSF attachment receptor) complex consisting of synaptobrevin2, SNAP25, and syntaxin1. These proteins are required for vesicle priming and fusion. We generated an improved SNAP25-based SNARE COmplex Reporter (SCORE2) incorporating mCeruelan3 and Venus and overexpressed it in SNAP25 knockout embryonic mouse chromaffin cells. This construct rescues vesicle fusion with properties indistinguishable from fusion in wild-type cells. Combining electrochemical imaging of individual release events using electrochemical detector arrays with total internal reflection fluorescence resonance energy transfer (TIR-FRET) imaging reveals a rapid FRET increase preceding individual fusion events by 65 ms. The experiments are performed under conditions of a steady-state cycle of docking, priming, and fusion, and the delay suggests that the FRET change reflects tight docking and priming of the vesicle, followed by fusion after ~65 ms. Given the absence of wt SNAP25, SCORE2 allows determination of the number of molecules at fusion sites and the number that changes conformation. The number of SNAP25 molecules changing conformation in the priming step increases with vesicle size and SNAP25 density in the plasma membrane and equals the number of copies present in the vesicle-plasma membrane contact zone. We estimate that in wt cells, 6 to 7 copies of SNAP25 change conformation during the priming step.
    MeSH term(s) Animals ; Mice ; Cell Membrane/metabolism ; Chromaffin Cells/metabolism ; Exocytosis/physiology ; Membrane Fusion/physiology ; SNARE Proteins/metabolism ; Synaptosomal-Associated Protein 25/genetics ; Synaptosomal-Associated Protein 25/metabolism
    Chemical Substances SNARE Proteins ; Synaptosomal-Associated Protein 25 ; Snap25 protein, mouse
    Language English
    Publishing date 2024-01-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2309161121
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1148: Show issues Location:
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  6. Article ; Online: Characterization of PROPPIN-Phosphoinositide Binding by Stopped-Flow Fluorescence Spectroscopy.

    Pérez-Lara, Ángel / Jahn, Reinhard

    Methods in molecular biology (Clifton, N.J.)

    2021  Volume 2251, Page(s) 205–214

    Abstract: PROPPINs (β-propellers that bind polyphosphoinositides) are a protein family that binds preferentially phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) via its FRRG motif. PROPPINs are involved in ... ...

    Abstract PROPPINs (β-propellers that bind polyphosphoinositides) are a protein family that binds preferentially phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) via its FRRG motif. PROPPINs are involved in autophagic functions, but their molecular mechanism is still elusive. To unravel the molecular mechanism of PROPPINs, it is essential to understand the PROPPIN-phosphoinositide binding. Here, we describe a protocol to study the kinetics of the PROPPIN-phosphoinositide binding using a fluorescence resonance energy transfer (FRET) stopped-flow approach. We use FRET between fluorophore-labeled protein and fluorophore-labeled liposomes, monitoring the increase of the acceptor emission in labeled liposomes after the protein-membrane binding. Through this approach, we studied the kinetics of the PROPPIN Atg18 (Autophagy-related protein 18) from Pichia angusta (PaAtg18) and a mutant of its FRRG motif, called FTTG mutant. Stopped-flow experiments demonstrated that the main function of the FRRG motif is to retain, instead of to drive, Atg18 to the membrane, decreasing the Atg18 dissociation rate. Furthermore, this method is suitable for the study of other PI-binding proteins.
    MeSH term(s) Autophagy ; Autophagy-Related Proteins/metabolism ; Autophagy-Related Proteins/pharmacokinetics ; Carrier Proteins/metabolism ; Fluorescence Resonance Energy Transfer/methods ; Membrane Proteins/metabolism ; Membrane Proteins/pharmacokinetics ; Phosphatidylinositol Phosphates/metabolism ; Phosphatidylinositols/metabolism ; Protein Binding/physiology ; Protein Conformation, beta-Strand/physiology ; Protein Domains/physiology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/pharmacokinetics ; Saccharomycetales/metabolism ; Spectrometry, Fluorescence/methods ; Vacuoles/metabolism
    Chemical Substances ATG18 protein, S cerevisiae ; Autophagy-Related Proteins ; Carrier Proteins ; Membrane Proteins ; Phosphatidylinositol Phosphates ; Phosphatidylinositols ; Saccharomyces cerevisiae Proteins ; phosphatidylinositol 3-phosphate
    Language English
    Publishing date 2021-01-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-1142-5_15
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Author Correction: Isolation of large dense-core vesicles from bovine adrenal medulla for functional studies.

    Birinci, Yelda / Preobraschenski, Julia / Ganzella, Marcelo / Jahn, Reinhard / Park, Yongsoo

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 16738

    Language English
    Publishing date 2022-10-06
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-022-21361-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Isolation of Synaptic Vesicles from Mammalian Brain.

    Ganzella, Marcelo / Ninov, Momchil / Riedel, Dietmar / Jahn, Reinhard

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2417, Page(s) 131–145

    Abstract: Synaptic vesicles (SVs) store neurotransmitters and undergo a fine-tuned regulatory and dynamic cycle of exo- and endocytosis, which is essential for neurotransmission at chemical synapses. The development of protocols for isolating SVs from biological ... ...

    Abstract Synaptic vesicles (SVs) store neurotransmitters and undergo a fine-tuned regulatory and dynamic cycle of exo- and endocytosis, which is essential for neurotransmission at chemical synapses. The development of protocols for isolating SVs from biological extracts was a fundamental accomplishment since it allowed for characterizing the molecular properties of SVs using biochemical methods. In this chapter, we describe a modified procedure for isolating SVs from a few g of rodent brain and that can be completed within ~12 h. The protocol involves the preparation of isolated nerve terminals from which SVs are released by osmotic shock and then enriched via various centrifugation steps, followed by size exclusion chromatography as final purification step. The final vesicle fraction is 22-fold enriched in SVs over the starting material, and the final yield of SVs obtained using this protocol is approximately 20 μg of protein per gram of mouse brain. The degree of contamination by other organelles and particles monitored by morphology and immunolabeling compares well with that of the classical protocols.
    MeSH term(s) Animals ; Brain/metabolism ; Mammals ; Mice ; Neurotransmitter Agents/metabolism ; Synapses/metabolism ; Synaptic Transmission ; Synaptic Vesicles/metabolism
    Chemical Substances Neurotransmitter Agents
    Language English
    Publishing date 2022-01-31
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-1916-2_11
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Book ; Online ; Thesis: Targeting ion sensors to synaptic vesicles using a Nanobody against luminal Synaptotagmin 1

    Goel, Rashi [Verfasser] / Jahn, Reinhard [Akademischer Betreuer] / Jahn, Reinhard [Gutachter] / Rizzoli, Silvio [Gutachter] / Steinem, Claudia [Gutachter]

    2022  

    Author's details Rashi Goel ; Gutachter: Reinhard Jahn, Silvio Rizzoli, Claudia Steinem ; Betreuer: Reinhard Jahn
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Niedersächsische Staats- und Universitätsbibliothek Göttingen
    Publishing place Göttingen
    Document type Book ; Online ; Thesis
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  10. Book ; Online ; Thesis: Kinetic analysis of neuronal SNARE protein interactions

    Pribicevic, Sonja [Verfasser] / Jahn, Reinhard Akademischer Betreuer] / Jahn, Reinhard [Gutachter] / Moser, Tobias [Gutachter] / [Rodnina, Marina [Gutachter]

    2022  

    Author's details Sonja Pribićević ; Gutachter: Reinhard Jahn, Tobias Moser, Marina Rodnina ; Betreuer: Reinhard Jahn
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Niedersächsische Staats- und Universitätsbibliothek Göttingen
    Publishing place Göttingen
    Document type Book ; Online ; Thesis
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