A BLOC-1–AP-3 super-complex sorts a cis-SNARE complex into endosome-derived tubular transport carriers

Autor: David J. Owen, Dorothy C. Bennett, Yueyao Zhu, Graça Raposo-Benedetti, Elena V. Sviderskaya, Shanna L. Bowman, Dawn C. Harper, Michael S. Marks, Linh Le, Megan K. Dennis, Alexander C. Theos, Anand Sitaram

Publikováno v: The Journal of Cell Biology

Bowman et al. show that in melanocytes, the vSNARE VAMP7 is sorted from endosomes into tubular membrane transport carriers bound for maturing melanosomes in a complex with the tSNARE syntaxin 13 via redundant recognition of each SNARE by an AP-3–BL

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9aa7f4a23cc4c5be5194f97dee3e6f5
http://europepmc.org/articles/PMC8077166

Tomosyn guides SNARE complex formation in coordination with Munc18 and Munc13

Autor: Le Zhu, Cong Ma, Tianzhi Li, Yun Li, Shen Wang

Publikováno v: FEBS Letters. 592:1161-1172

As a SNARE binding protein, tomosyn has been reported to negatively regulate synaptic exocytosis via arresting syntaxin-1 and SNAP-25 into a nonfusogenic product that precludes synaptobrevin-2 entry, raising the question how the assembly of the SNARE

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7762889f9368613df31dc43d98a1796
https://doi.org/10.1002/1873-3468.13018

Tomosyn functions as a PKCδ-regulated fusion clamp in mast cell degranulation

Autor: Marc Benhamou, Luca Danelli, Nicolas Charles, Joana Vitte, Claudia González-Espinosa, C. Agabriel, Emeline Pacreau, C. Klingebiel, Gaël Ménasché, Marina Macías-Silva, Bárbara Dema, Iris K. Madera-Salcedo, Joëlle Birnbaum, V. Liabeuf, Neeraj Tiwari, Ulrich Blank, Shamila Vibhushan

Publikováno v: Science Signaling
Science Signaling, 2018, 11 (537), pp.eaan4350. ⟨10.1126/scisignal.aan4350⟩
Science Signaling, American Association for the Advancement of Science, 2018, 11 (537), pp.eaan4350. ⟨10.1126/scisignal.aan4350⟩
Science Signaling, American Association for the Advancement of Science, 2018, 11 (537), ⟨10.1126/scisignal.aan4350⟩
Science Signaling, 2018, 11 (537), ⟨10.1126/scisignal.aan4350⟩

International audience; Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family proteins mediate membrane fusion critical for vesicular transport and cellular secretion. Mast cells rely on SNARE-mediated membrane fusion f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fd9d2969a064e5a23a9e8aaf49054f9
https://www.hal.inserm.fr/inserm-02323254/file/eaan4350.full.pdf

Synaptotagmin-1 binds to PIP2-containing membrane but not to SNAREs at physiological ionic strength

Autor: Seung-Ryoung Jung, M. Y. Choi, Iman Kattan, David S. Cafiso, Kyungreem Han, Ángel Pérez-Lara, Jong Bae Seo, Reinhard Jahn, Yongsoo Park, Peter Walla, Halenur Yavuz, Alicia M. Fraind, Duk Su Koh

Publikováno v: Nature structural & molecular biology
Nature Structural and Molecular Biology

The Ca(2+) sensor synaptotagmin-1 is thought to trigger membrane fusion by binding to acidic membrane lipids and SNARE proteins. Previous work has shown that binding is mediated by electrostatic interactions that are sensitive to the ionic environmen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3053bd99f0a2403a98a485e0e6e36577
https://doi.org/10.1038/nsmb.3097

A synaptotagmin suppressor screen indicates SNARE binding controls the timing and Ca2+ cooperativity of vesicle fusion

Autor: Roger Bryan Sutton, J. Troy Littleton, Maria Bykhovskaia, Ramon A. Jorquera, Zhuo Guan, Yulia Akbergenova

Publikováno v: eLife, Vol 6 (2017)

The synaptic vesicle Ca2+ sensor Synaptotagmin binds Ca2+ through its two C2 domains to trigger membrane interactions. Beyond membrane insertion by the C2 domains, other requirements for Synaptotagmin activity are still being elucidated. To identify

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9da96e5b8bf5e5bde893b1563ab5f11c
https://doi.org/10.7554/elife.28409