A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis

Autor: Wanlu Zhang, Azqa Khan, Jlenia Vitale, Annett Neuner, Kerstin Rink, Christian Lüchtenborg, Britta Brügger, Thomas H. Söllner, Elmar Schiebel

Publikováno v: Open Biology, Vol 11, Iss 11 (2021)

The integral membrane protein Apq12 is an important nuclear envelope (NE)/endoplasmic reticulum (ER) modulator that cooperates with the nuclear pore complex (NPC) biogenesis factors Brl1 and Brr6. How Apq12 executes these functions is unknown. Here,

Externí odkaz: https://doaj.org/article/49f2b3970e5e42359e25debff6fe7f98

Electrostatic anchoring precedes stable membrane attachment of SNAP25/SNAP23 to the plasma membrane

Autor: Pascal Weber, Helena Batoulis, Kerstin M Rink, Stefan Dahlhoff, Kerstin Pinkwart, Thomas H Söllner, Thorsten Lang

Publikováno v: eLife, Vol 6 (2017)

The SNAREs SNAP25 and SNAP23 are proteins that are initially cytosolic after translation, but then become stably attached to the cell membrane through palmitoylation of cysteine residues. For palmitoylation to occur, membrane association is a prerequ

Externí odkaz: https://doaj.org/article/298535a8282949ea848d29c92c1919ca

A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis

Autor: Christian Lüchtenborg, Wanlu Zhang, Kerstin M Rink, Annett Neuner, Elmar Schiebel, Azqa Khan, Thomas H. Söllner, Britta Brügger, Jlenia Vitale

Publikováno v: Open Biology, Vol 11, Iss 11 (2021)
Open Biology

The integral membrane protein Apq12 is an important nuclear envelope (NE)/endoplasmic reticulum (ER) modulator that cooperates with the nuclear pore complex (NPC) biogenesis factors Brl1 and Brr6. How Apq12 executes these functions is unknown. Here,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaa5fc7d88c83a032324bd4176975b8c
https://doi.org/10.1098/rsob.210250

Tyrosine phosphorylation of Munc18-1 inhibits synaptic transmission by preventing SNARE assembly

Autor: Ruud F. Toonen, Jan R.T. van Weering, Thomas H. Söllner, Matthijs Verhage, Bernhard Dörr, Chrysanthi Blithikioti, Marieke Meijer, Hanna C.A. Lammertse

Publikováno v: Meijer, M, Dörr, B, Lammertse, H C, Blithikioti, C, van Weering, J R, Toonen, R F, Söllner, T H & Verhage, M 2018, ' Tyrosine phosphorylation of Munc18-1 inhibits synaptic transmission by preventing SNARE assembly ', EMBO Journal, vol. 37, no. 2, pp. 300-320 . https://doi.org/10.15252/embj.201796484
EMBO Journal, 37(2), 300-320. Nature Publishing Group
Meijer, M, Dörr, B, Lammertse, H C A, Blithikioti, C, van Weering, J R T, Toonen, R F G, Söllner, T H & Verhage, M 2018, ' Tyrosine phosphorylation of Munc18-1 inhibits synaptic transmission by preventing SNARE assembly ', EMBO Journal, vol. 37, no. 2, pp. 300-320 . https://doi.org/10.15252/embj.201796484
EMBO Journal, 37(2), 300-320. Wiley-Blackwell
The EMBO Journal

Tyrosine kinases are important regulators of synaptic strength. Here, we describe a key component of the synaptic vesicle release machinery, Munc18-1, as a phosphorylation target for neuronal Src family kinases (SFKs). Phosphomimetic Y473D mutation o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e71aa215665664fa02788d66552de25d
https://doi.org/10.15252/embj.201796484

Interactions Between SNAP-25 and Synaptotagmin-1 Are Involved in Vesicle Priming, Clamping Spontaneous and Stimulating Evoked Neurotransmission

Autor: Andrea Scheutzow, Keimpe D. Wierda, Jakob B. Sørensen, Jörg Malsam, Thomas H. Söllner, Melanie Schupp, Marvin Ruiter

Publikováno v: The Journal of Neuroscience. 36:11865-11880

Whether interactions between synaptotagmin-1 (syt-1) and the soluble NSF attachment protein receptors (SNAREs) are required during neurotransmission is debated. We examined five SNAP-25 mutations designed to interfere with syt-1 interactions. One mut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98901948b0cd9bf746ac4927ed00e541
https://doi.org/10.1523/jneurosci.1011-16.2016