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  1. Article ; Online: Synaptobrevin-2 C-Terminal Flexible Region Regulates the Discharge of Catecholamine Molecules.

    Weiss, Annita N

    Biophysical journal

    2019  Volume 116, Issue 5, Page(s) 921–929

    Abstract: The discharge of neurotransmitters from vesicles is a regulated process. Synaptobrevin-2, a snap receptor (SNARE) protein, participates in this process by interacting with other SNARE and associated proteins. Synaptobrevin-2 transmembrane domain is ... ...

    Abstract The discharge of neurotransmitters from vesicles is a regulated process. Synaptobrevin-2, a snap receptor (SNARE) protein, participates in this process by interacting with other SNARE and associated proteins. Synaptobrevin-2 transmembrane domain is embedded into the vesicle lipid bilayer except for its last three residues. These residues are hydrophilic and constitute synaptobrevin-2 C-terminal flexible region. The residue Y113 of synaptobrevin-2 flexible region was mutated to lysine and glutamate. The effects of these mutations on the exocytotic process in chromaffin cells were assessed using capacitance measurements combined with amperometry and stimulation by flash photolysis of caged Ca
    MeSH term(s) Catecholamines/metabolism ; Chromaffin Cells/metabolism ; Models, Molecular ; Protein Conformation ; Vesicle-Associated Membrane Protein 2/chemistry ; Vesicle-Associated Membrane Protein 2/metabolism
    Chemical Substances Catecholamines ; Vesicle-Associated Membrane Protein 2
    Language English
    Publishing date 2019-02-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2019.01.028
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: The SNARE protein vti1a functions in dense-core vesicle biogenesis.

    Walter, Alexander M / Kurps, Julia / de Wit, Heidi / Schöning, Susanne / Toft-Bertelsen, Trine L / Lauks, Juliane / Ziomkiewicz, Iwona / Weiss, Annita N / Schulz, Alexander / Fischer von Mollard, Gabriele / Verhage, Matthijs / Sørensen, Jakob B

    The EMBO journal

    2014  Volume 33, Issue 15, Page(s) 1681–1697

    Abstract: The SNARE protein vti1a is proposed to drive fusion of intracellular organelles, but recent data also implicated vti1a in exocytosis. Here we show that vti1a is absent from mature secretory vesicles in adrenal chromaffin cells, but localizes to a ... ...

    Abstract The SNARE protein vti1a is proposed to drive fusion of intracellular organelles, but recent data also implicated vti1a in exocytosis. Here we show that vti1a is absent from mature secretory vesicles in adrenal chromaffin cells, but localizes to a compartment near the trans-Golgi network, partially overlapping with syntaxin-6. Exocytosis is impaired in vti1a null cells, partly due to fewer Ca(2+)-channels at the plasma membrane, partly due to fewer vesicles of reduced size and synaptobrevin-2 content. In contrast, release kinetics and Ca(2+)-sensitivity remain unchanged, indicating that the final fusion reaction leading to transmitter release is unperturbed. Additional deletion of the closest related SNARE, vti1b, does not exacerbate the vti1a phenotype, and vti1b null cells show no secretion defects, indicating that vti1b does not participate in exocytosis. Long-term re-expression of vti1a (days) was necessary for restoration of secretory capacity, whereas strong short-term expression (hours) was ineffective, consistent with vti1a involvement in an upstream step related to vesicle generation, rather than in fusion. We conclude that vti1a functions in vesicle generation and Ca(2+)-channel trafficking, but is dispensable for transmitter release.
    MeSH term(s) Animals ; Calcium Channels/metabolism ; Cell Nucleus Structures/metabolism ; Chromaffin Cells/metabolism ; Exocytosis/physiology ; Mice ; Mice, Mutant Strains ; Qa-SNARE Proteins/metabolism ; Qb-SNARE Proteins/genetics ; Qb-SNARE Proteins/metabolism ; Secretory Vesicles/metabolism ; Vesicle-Associated Membrane Protein 2/metabolism
    Chemical Substances Calcium Channels ; Qa-SNARE Proteins ; Qb-SNARE Proteins ; Vesicle-Associated Membrane Protein 2 ; Vti1a protein, mouse ; Vti1b protein, mouse
    Language English
    Publishing date 2014-06-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.201387549
    Database MEDical Literature Analysis and Retrieval System OnLINE

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